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Protein

Malate synthase G

Gene

glcB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: 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.UniRule annotation3 Publications

Catalytic activityi

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

Cofactori

Mg2+UniRule annotation1 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)1 Publication
  1. Vmax=36.1 µmol/min/mg enzyme (at pH 8 and 37 degrees Celsius)1 Publication

Pathwayi: glyoxylate cycle

This protein is involved in step 2 of the subpathway that synthesizes (S)-malate from isocitrate.UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Isocitrate lyase (aceA)
  2. Malate synthase G (glcB), Malate synthase A (aceB)
This subpathway is part of the pathway glyoxylate cycle, which is itself part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-malate from isocitrate, the pathway glyoxylate cycle and in Carbohydrate metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei118Acetyl-CoA; via carbonyl oxygen1
Binding sitei274Acetyl-CoA1
Binding sitei311Acetyl-CoA1
Active sitei338Proton acceptor1
Binding sitei338Glyoxylate1
Metal bindingi427Magnesium1
Binding sitei427Glyoxylate1
Metal bindingi455Magnesium1
Binding sitei536Acetyl-CoA; via carbonyl oxygen1
Active sitei631Proton donor1

GO - Molecular functioni

  • malate synthase activity Source: EcoCyc
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • glyoxylate catabolic process Source: EcoCyc
  • glyoxylate cycle Source: GO_Central
  • 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.
BRENDAi2.3.3.9. 2026.
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG20080. glcB.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
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)DescriptionActionsGraphical viewLength
Mutagenesisi338R → K: Has a specific activity which is only 6.6% of the wild-type activity. 1 Publication1
Mutagenesisi617C → S: Affinity binding for acetyl-CoA is more than five times greater than that of wild-type, although its specific activity is comparable. 1 Publication1
Mutagenesisi631D → N: Absence of malate synthase activity. 1 Publication1

Chemistry databases

DrugBankiDB01638. D-Sorbitol.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001668862 – 723Malate synthase GAdd BLAST722

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei617Cysteine sulfenic acid (-SOH)UniRule annotation1 Publication1
Modified residuei688Cysteine sulfenic acid (-SOH)UniRule annotation1 Publication1

Keywords - PTMi

Oxidation

Proteomic databases

EPDiP37330.
PaxDbiP37330.
PRIDEiP37330.

Expressioni

Inductioni

By glycolate.3 Publications

Interactioni

Subunit structurei

Monomer.UniRule annotation4 Publications

Protein-protein interaction databases

BioGridi4259239. 14 interactors.
DIPiDIP-9761N.
IntActiP37330. 6 interactors.
MINTiMINT-1248166.
STRINGi511145.b2976.

Structurei

Secondary structure

1723
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 7Combined sources3
Beta strandi10 – 12Combined sources3
Helixi14 – 23Combined sources10
Helixi25 – 28Combined sources4
Helixi32 – 70Combined sources39
Beta strandi74 – 76Combined sources3
Helixi78 – 87Combined sources10
Helixi107 – 110Combined sources4
Beta strandi116 – 120Combined sources5
Helixi124 – 131Combined sources8
Helixi132 – 134Combined sources3
Beta strandi135 – 137Combined sources3
Helixi138 – 143Combined sources6
Beta strandi145 – 148Combined sources4
Beta strandi152 – 154Combined sources3
Beta strandi155 – 157Combined sources3
Helixi160 – 177Combined sources18
Beta strandi180 – 183Combined sources4
Helixi185 – 187Combined sources3
Beta strandi188 – 194Combined sources7
Beta strandi197 – 202Combined sources6
Beta strandi207 – 212Combined sources6
Helixi213 – 215Combined sources3
Beta strandi216 – 222Combined sources7
Beta strandi225 – 233Combined sources9
Beta strandi236 – 242Combined sources7
Helixi249 – 251Combined sources3
Beta strandi256 – 262Combined sources7
Beta strandi265 – 272Combined sources8
Helixi280 – 294Combined sources15
Beta strandi299 – 301Combined sources3
Turni305 – 307Combined sources3
Beta strandi310 – 312Combined sources3
Beta strandi317 – 321Combined sources5
Beta strandi326 – 329Combined sources4
Beta strandi331 – 333Combined sources3
Beta strandi334 – 338Combined sources5
Beta strandi345 – 350Combined sources6
Beta strandi356 – 358Combined sources3
Helixi359 – 377Combined sources19
Beta strandi382 – 384Combined sources3
Beta strandi386 – 390Combined sources5
Helixi396 – 412Combined sources17
Beta strandi420 – 426Combined sources7
Helixi429 – 432Combined sources4
Helixi435 – 440Combined sources6
Turni441 – 445Combined sources5
Beta strandi446 – 451Combined sources6
Helixi453 – 463Combined sources11
Helixi465 – 467Combined sources3
Helixi473 – 475Combined sources3
Helixi480 – 495Combined sources16
Turni499 – 501Combined sources3
Beta strandi502 – 506Combined sources5
Helixi515 – 521Combined sources7
Helixi523 – 527Combined sources5
Beta strandi531 – 537Combined sources7
Helixi538 – 550Combined sources13
Helixi553 – 560Combined sources8
Helixi565 – 576Combined sources12
Helixi589 – 613Combined sources25
Beta strandi618 – 621Combined sources4
Beta strandi627 – 630Combined sources4
Helixi632 – 647Combined sources16
Turni648 – 650Combined sources3
Helixi653 – 670Combined sources18
Turni671 – 673Combined sources3
Beta strandi674 – 676Combined sources3
Turni680 – 683Combined sources4
Helixi684 – 686Combined sources3
Helixi688 – 698Combined sources11
Helixi700 – 702Combined sources3
Helixi704 – 706Combined sources3
Helixi709 – 720Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1D8CX-ray2.00A1-723[»]
1P7TX-ray1.95A/B3-723[»]
1Y8BNMR-A1-723[»]
2JQXNMR-A1-723[»]
ProteinModelPortaliP37330.
SMRiP37330.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP37330.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni125 – 126Acetyl-CoA binding2
Regioni452 – 455Glyoxylate binding4

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4107QP3. Bacteria.
COG2225. LUCA.
HOGENOMiHOG000220740.
InParanoidiP37330.
KOiK01638.
OMAiGYNEVRG.
PhylomeDBiP37330.

Family and domain databases

CDDicd00728. malate_synt_G. 1 hit.
Gene3Di2.170.170.11. 2 hits.
HAMAPiMF_00641. Malate_synth_G. 1 hit.
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.
WP_000084131.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76012; AAC76012; b2976.
BAE77036; BAE77036; BAE77036.
GeneIDi948857.
KEGGiecj:JW2943.
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.
PIRiS51788.
RefSeqiNP_417450.1. NC_000913.3.
WP_000084131.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1D8CX-ray2.00A1-723[»]
1P7TX-ray1.95A/B3-723[»]
1Y8BNMR-A1-723[»]
2JQXNMR-A1-723[»]
ProteinModelPortaliP37330.
SMRiP37330.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259239. 14 interactors.
DIPiDIP-9761N.
IntActiP37330. 6 interactors.
MINTiMINT-1248166.
STRINGi511145.b2976.

Chemistry databases

DrugBankiDB01638. D-Sorbitol.

Proteomic databases

EPDiP37330.
PaxDbiP37330.
PRIDEiP37330.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76012; AAC76012; b2976.
BAE77036; BAE77036; BAE77036.
GeneIDi948857.
KEGGiecj:JW2943.
eco:b2976.
PATRICi32121366. VBIEscCol129921_3070.

Organism-specific databases

EchoBASEiEB4141.
EcoGeneiEG20080. glcB.

Phylogenomic databases

eggNOGiENOG4107QP3. Bacteria.
COG2225. LUCA.
HOGENOMiHOG000220740.
InParanoidiP37330.
KOiK01638.
OMAiGYNEVRG.
PhylomeDBiP37330.

Enzyme and pathway databases

UniPathwayiUPA00703; UER00720.
BioCyciEcoCyc:MALSYNG-MONOMER.
ECOL316407:JW2943-MONOMER.
MetaCyc:MALSYNG-MONOMER.
BRENDAi2.3.3.9. 2026.

Miscellaneous databases

EvolutionaryTraceiP37330.
PROiP37330.

Family and domain databases

CDDicd00728. malate_synt_G. 1 hit.
Gene3Di2.170.170.11. 2 hits.
HAMAPiMF_00641. Malate_synth_G. 1 hit.
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.
ProtoNetiSearch...

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 30, 2016
This is version 147 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.