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

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 PublicationsUniRule annotation

Catalytic activityi

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

Cofactori

Mg2+1 PublicationUniRule annotation

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)1 Publication

Vmax=36.1 µmol/min/mg enzyme (at pH 8 and 37 degrees Celsius)1 Publication

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 acceptor
Binding sitei338 – 3381Glyoxylate
Metal bindingi427 – 4271Magnesium
Binding sitei427 – 4271Glyoxylate
Metal bindingi455 – 4551Magnesium
Binding sitei536 – 5361Acetyl-CoA; via carbonyl oxygen
Active sitei631 – 6311Proton donor

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 GUniRule annotation (EC:2.3.3.9UniRule annotation)
Short name:
MSG
Gene namesi
Name:glcBUniRule annotation
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

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
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 GPRO_0000166886Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei617 – 6171Cysteine sulfenic acid (-SOH)1 PublicationUniRule annotation
Modified residuei688 – 6881Cysteine sulfenic acid (-SOH)1 PublicationUniRule annotation

Keywords - PTMi

Oxidation

Proteomic databases

PaxDbiP37330.
PRIDEiP37330.

Expressioni

Inductioni

By glycolate.3 Publications

Gene expression databases

GenevestigatoriP37330.

Interactioni

Subunit structurei

Monomer.4 PublicationsUniRule annotation

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP37330.

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the malate synthase family. GlcB subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG2225.
HOGENOMiHOG000220740.
InParanoidiP37330.
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

        10         20         30         40         50
MSQTITQSRL RIDANFKRFV DEEVLPGTGL DAAAFWRNFD EIVHDLAPEN
60 70 80 90 100
RQLLAERDRI QAALDEWHRS NPGPVKDKAA YKSFLRELGY LVPQPERVTV
110 120 130 140 150
ETTGIDSEIT SQAGPQLVVP AMNARYALNA ANARWGSLYD ALYGSDIIPQ
160 170 180 190 200
EGAMVSGYDP QRGEQVIAWV RRFLDESLPL ENGSYQDVVA FKVVDKQLRI
210 220 230 240 250
QLKNGKETTL RTPAQFVGYR GDAAAPTCIL LKNNGLHIEL QIDANGRIGK
260 270 280 290 300
DDPAHINDVI VEAAISTILD CEDSVAAVDA EDKILLYRNL LGLMQGTLQE
310 320 330 340 350
KMEKNGRQIV RKLNDDRHYT AADGSEISLH GRSLLFIRNV GHLMTIPVIW
360 370 380 390 400
DSEGNEIPEG ILDGVMTGAI ALYDLKVQKN SRTGSVYIVK PKMHGPQEVA
410 420 430 440 450
FANKLFTRIE TMLGMAPNTL KMGIMDEERR TSLNLRSCIA QARNRVAFIN
460 470 480 490 500
TGFLDRTGDE MHSVMEAGPM LRKNQMKSTP WIKAYERNNV LSGLFCGLRG
510 520 530 540 550
KAQIGKGMWA MPDLMADMYS QKGDQLRAGA NTAWVPSPTA ATLHALHYHQ
560 570 580 590 600
TNVQSVQANI AQTEFNAEFE PLLDDLLTIP VAENANWSAQ EIQQELDNNV
610 620 630 640 650
QGILGYVVRW VEQGIGCSKV PDIHNVALME DRATLRISSQ HIANWLRHGI
660 670 680 690 700
LTKEQVQASL ENMAKVVDQQ NAGDPAYRPM AGNFANSCAF KAASDLIFLG
710 720
VKQPNGYTEP LLHAWRLREK ESH
Length:723
Mass (Da):80,489
Last modified:January 23, 2007 - v3
Checksum:i820F177D3FE02632
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
InParanoidi P37330.
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, OXIDATION AT CYS-617 AND CYS-688, 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: November 26, 2014
This is version 133 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