SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P37330

- MASZ_ECOLI

UniProt

P37330 - MASZ_ECOLI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Malate synthase G

Gene
glcB, glc, b2976, JW2943
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form malate and CoA.3 Publications

Catalytic activityi

Acetyl-CoA + H2O + glyoxylate = (S)-malate + CoA.UniRule annotation

Cofactori

Magnesium.1 Publication

Kineticsi

Kcat is 48.1 sec(-1) for glyoxylate (at pH 8 and 37 degrees Celsius).

  1. KM=9 µM for acetyl-CoA (at pH 8 and 37 degrees Celsius)1 Publication
  2. KM=21 µM for glyoxylate (at pH 8 and 37 degrees Celsius)

Vmax=36.1 µmol/min/mg enzyme (at pH 8 and 37 degrees Celsius)

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei118 – 1181Acetyl-CoA; via carbonyl oxygen
Binding sitei274 – 2741Acetyl-CoA
Binding sitei311 – 3111Acetyl-CoA
Active sitei338 – 3381Proton acceptor2 Publications
Binding sitei338 – 3381Glyoxylate
Metal bindingi427 – 4271Magnesium
Binding sitei427 – 4271Glyoxylate
Metal bindingi455 – 4551Magnesium
Binding sitei536 – 5361Acetyl-CoA; via carbonyl oxygen
Active sitei631 – 6311Proton donor2 Publications

GO - Molecular functioni

  1. malate synthase activity Source: EcoCyc
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. glyoxylate catabolic process Source: EcoCyc
  2. glyoxylate cycle Source: UniProtKB-HAMAP
  3. tricarboxylic acid cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Glyoxylate bypass, Tricarboxylic acid cycle

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:MALSYNG-MONOMER.
ECOL316407:JW2943-MONOMER.
MetaCyc:MALSYNG-MONOMER.
UniPathwayiUPA00703; UER00720.

Names & Taxonomyi

Protein namesi
Recommended name:
Malate synthase G (EC:2.3.3.9)
Short name:
MSG
Gene namesi
Name:glcB
Synonyms:glc
Ordered Locus Names:b2976, JW2943
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG20080. glcB.

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene are unable to oxidize glyoxylate.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi338 – 3381R → K: Has a specific activity which is only 6.6% of the wild-type activity. 1 Publication
Mutagenesisi617 – 6171C → S: Affinity binding for acetyl-CoA is more than five times greater than that of wild-type, although its specific activity is comparable. 1 Publication
Mutagenesisi631 – 6311D → N: Absence of malate synthase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 723722Malate synthase GUniRule annotationPRO_0000166886Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei617 – 6171Cysteine sulfenic acid (-SOH)UniRule annotation
Modified residuei688 – 6881Cysteine sulfenic acid (-SOH)UniRule annotation

Keywords - PTMi

Oxidation

Proteomic databases

PaxDbiP37330.
PRIDEiP37330.

Expressioni

Inductioni

By glycolate.3 Publications

Gene expression databases

GenevestigatoriP37330.

Interactioni

Subunit structurei

Monomer.3 Publications

Protein-protein interaction databases

DIPiDIP-9761N.
IntActiP37330. 6 interactions.
MINTiMINT-1248166.
STRINGi511145.b2976.

Structurei

Secondary structure

1
723
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 73
Beta strandi10 – 123
Helixi14 – 2310
Helixi25 – 284
Helixi32 – 7039
Beta strandi74 – 763
Helixi78 – 8710
Helixi107 – 1104
Beta strandi116 – 1205
Helixi124 – 1318
Helixi132 – 1343
Beta strandi135 – 1373
Helixi138 – 1436
Beta strandi145 – 1484
Beta strandi152 – 1543
Beta strandi155 – 1573
Helixi160 – 17718
Beta strandi180 – 1834
Helixi185 – 1873
Beta strandi188 – 1947
Beta strandi197 – 2026
Beta strandi207 – 2126
Helixi213 – 2153
Beta strandi216 – 2227
Beta strandi225 – 2339
Beta strandi236 – 2427
Helixi249 – 2513
Beta strandi256 – 2627
Beta strandi265 – 2728
Helixi280 – 29415
Beta strandi299 – 3013
Turni305 – 3073
Beta strandi310 – 3123
Beta strandi317 – 3215
Beta strandi326 – 3294
Beta strandi331 – 3333
Beta strandi334 – 3385
Beta strandi345 – 3506
Beta strandi356 – 3583
Helixi359 – 37719
Beta strandi382 – 3843
Beta strandi386 – 3905
Helixi396 – 41217
Beta strandi420 – 4267
Helixi429 – 4324
Helixi435 – 4406
Turni441 – 4455
Beta strandi446 – 4516
Helixi453 – 46311
Helixi465 – 4673
Helixi473 – 4753
Helixi480 – 49516
Turni499 – 5013
Beta strandi502 – 5065
Helixi515 – 5217
Helixi523 – 5275
Beta strandi531 – 5377
Helixi538 – 55013
Helixi553 – 5608
Helixi565 – 57612
Helixi589 – 61325
Beta strandi618 – 6214
Beta strandi627 – 6304
Helixi632 – 64716
Turni648 – 6503
Helixi653 – 67018
Turni671 – 6733
Beta strandi674 – 6763
Turni680 – 6834
Helixi684 – 6863
Helixi688 – 69811
Helixi700 – 7023
Helixi704 – 7063
Helixi709 – 72012

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D8CX-ray2.00A1-723[»]
1P7TX-ray1.95A/B3-723[»]
1Y8BNMR-A1-723[»]
2JQXNMR-A1-723[»]
ProteinModelPortaliP37330.
SMRiP37330. Positions 1-723.

Miscellaneous databases

EvolutionaryTraceiP37330.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni125 – 1262Acetyl-CoA bindingUniRule annotation
Regioni452 – 4554Glyoxylate bindingUniRule annotation

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2225.
HOGENOMiHOG000220740.
KOiK01638.
OMAiPANTLKM.
OrthoDBiEOG6HJ286.
PhylomeDBiP37330.

Family and domain databases

Gene3Di2.170.170.11. 2 hits.
HAMAPiMF_00641. Malate_synth_G.
InterProiIPR011076. Malate_synth-like.
IPR023310. Malate_synth_G_beta_sub_dom.
IPR001465. Malate_synthase.
IPR006253. Malate_synthG.
[Graphical view]
PfamiPF01274. Malate_synthase. 1 hit.
[Graphical view]
SUPFAMiSSF51645. SSF51645. 1 hit.
TIGRFAMsiTIGR01345. malate_syn_G. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P37330-1 [UniParc]FASTAAdd to Basket

« Hide

MSQTITQSRL RIDANFKRFV DEEVLPGTGL DAAAFWRNFD EIVHDLAPEN    50
RQLLAERDRI QAALDEWHRS NPGPVKDKAA YKSFLRELGY LVPQPERVTV 100
ETTGIDSEIT SQAGPQLVVP AMNARYALNA ANARWGSLYD ALYGSDIIPQ 150
EGAMVSGYDP QRGEQVIAWV RRFLDESLPL ENGSYQDVVA FKVVDKQLRI 200
QLKNGKETTL RTPAQFVGYR GDAAAPTCIL LKNNGLHIEL QIDANGRIGK 250
DDPAHINDVI VEAAISTILD CEDSVAAVDA EDKILLYRNL LGLMQGTLQE 300
KMEKNGRQIV RKLNDDRHYT AADGSEISLH GRSLLFIRNV GHLMTIPVIW 350
DSEGNEIPEG ILDGVMTGAI ALYDLKVQKN SRTGSVYIVK PKMHGPQEVA 400
FANKLFTRIE TMLGMAPNTL KMGIMDEERR TSLNLRSCIA QARNRVAFIN 450
TGFLDRTGDE MHSVMEAGPM LRKNQMKSTP WIKAYERNNV LSGLFCGLRG 500
KAQIGKGMWA MPDLMADMYS QKGDQLRAGA NTAWVPSPTA ATLHALHYHQ 550
TNVQSVQANI AQTEFNAEFE PLLDDLLTIP VAENANWSAQ EIQQELDNNV 600
QGILGYVVRW VEQGIGCSKV PDIHNVALME DRATLRISSQ HIANWLRHGI 650
LTKEQVQASL ENMAKVVDQQ NAGDPAYRPM AGNFANSCAF KAASDLIFLG 700
VKQPNGYTEP LLHAWRLREK ESH 723
Length:723
Mass (Da):80,489
Last modified:January 23, 2007 - v3
Checksum:i820F177D3FE02632
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X74547 Genomic DNA. Translation: CAA52639.1.
U28377 Genomic DNA. Translation: AAA69143.1.
U00096 Genomic DNA. Translation: AAC76012.1.
AP009048 Genomic DNA. Translation: BAE77036.1.
PIRiS51788.
RefSeqiNP_417450.1. NC_000913.3.
YP_491172.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76012; AAC76012; b2976.
BAE77036; BAE77036; BAE77036.
GeneIDi12930245.
948857.
KEGGiecj:Y75_p2904.
eco:b2976.
PATRICi32121366. VBIEscCol129921_3070.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X74547 Genomic DNA. Translation: CAA52639.1 .
U28377 Genomic DNA. Translation: AAA69143.1 .
U00096 Genomic DNA. Translation: AAC76012.1 .
AP009048 Genomic DNA. Translation: BAE77036.1 .
PIRi S51788.
RefSeqi NP_417450.1. NC_000913.3.
YP_491172.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1D8C X-ray 2.00 A 1-723 [» ]
1P7T X-ray 1.95 A/B 3-723 [» ]
1Y8B NMR - A 1-723 [» ]
2JQX NMR - A 1-723 [» ]
ProteinModelPortali P37330.
SMRi P37330. Positions 1-723.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-9761N.
IntActi P37330. 6 interactions.
MINTi MINT-1248166.
STRINGi 511145.b2976.

Proteomic databases

PaxDbi P37330.
PRIDEi P37330.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76012 ; AAC76012 ; b2976 .
BAE77036 ; BAE77036 ; BAE77036 .
GeneIDi 12930245.
948857.
KEGGi ecj:Y75_p2904.
eco:b2976.
PATRICi 32121366. VBIEscCol129921_3070.

Organism-specific databases

EchoBASEi EB4141.
EcoGenei EG20080. glcB.

Phylogenomic databases

eggNOGi COG2225.
HOGENOMi HOG000220740.
KOi K01638.
OMAi PANTLKM.
OrthoDBi EOG6HJ286.
PhylomeDBi P37330.

Enzyme and pathway databases

UniPathwayi UPA00703 ; UER00720 .
BioCyci EcoCyc:MALSYNG-MONOMER.
ECOL316407:JW2943-MONOMER.
MetaCyc:MALSYNG-MONOMER.

Miscellaneous databases

EvolutionaryTracei P37330.
PROi P37330.

Gene expression databases

Genevestigatori P37330.

Family and domain databases

Gene3Di 2.170.170.11. 2 hits.
HAMAPi MF_00641. Malate_synth_G.
InterProi IPR011076. Malate_synth-like.
IPR023310. Malate_synth_G_beta_sub_dom.
IPR001465. Malate_synthase.
IPR006253. Malate_synthG.
[Graphical view ]
Pfami PF01274. Malate_synthase. 1 hit.
[Graphical view ]
SUPFAMi SSF51645. SSF51645. 1 hit.
TIGRFAMsi TIGR01345. malate_syn_G. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular characterization of Escherichia coli malate synthase G. Differentiation with the malate synthase A isoenzyme."
    Molina I., Badia J., Aguilar J.T., Pellicer M.T., Baldoma L.
    Eur. J. Biochem. 224:541-548(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-13, FUNCTION, SUBUNIT, INDUCTION, NOMENCLATURE.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Regulation of glyoxylate metabolism in Escherichia coli K-12."
    Ornston L.N., Ornston M.K.
    J. Bacteriol. 98:1098-1108(1969) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, INDUCTION.
  5. "Demonstration of 2 malate synthases in Escherichia coli."
    Falmagne P., Vanderwinkel E., Wiame J.M.
    Biochim. Biophys. Acta 99:246-258(1965) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Cross-induction of glc and ace operons of Escherichia coli attributable to pathway intersection. Characterization of the glc promoter."
    Pellicer M.T., Fernandez C., Badia J., Aguilar J., Lin E.C., Baldom L.
    J. Biol. Chem. 274:1745-1752(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  7. "Crystal structure of Escherichia coli malate synthase G complexed with magnesium and glyoxylate at 2.0-A resolution: mechanistic implications."
    Howard B.R., Endrizzi J.A., Remington S.J.
    Biochemistry 39:3156-3168(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND MAGNESIUM ION, ACTIVE SITE, COFACTOR, REACTION MECHANISM, SUBUNIT.
  8. "Structure of the Escherichia coli malate synthase G:pyruvate:acetyl-coenzyme A abortive ternary complex at 1.95 A resolution."
    Anstrom D.M., Kallio K., Remington S.J.
    Protein Sci. 12:1822-1832(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 3-722 IN COMPLEX WITH SUBSTRATE ANALOGS AND MAGNESIUM ION, MUTAGENESIS OF ARG-338; CYS-617 AND ASP-631, ACTIVE SITE, BIOPHYSICOCHEMICAL PROPERTIES.
  9. "Solution NMR-derived global fold of a monomeric 82-kDa enzyme."
    Tugarinov V., Choy W.Y., Orekhov V.Y., Kay L.E.
    Proc. Natl. Acad. Sci. U.S.A. 102:622-627(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 3-722, SUBUNIT.
  10. "Refined solution structure of the 82-kDa enzyme malate synthase G from joint NMR and synchrotron SAXS restraints."
    Grishaev A., Tugarinov V., Kay L.E., Trewhella J., Bax A.
    J. Biomol. NMR 40:95-106(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 3-723.

Entry informationi

Entry nameiMASZ_ECOLI
AccessioniPrimary (citable) accession number: P37330
Secondary accession number(s): Q2M9M0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 130 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi