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Protein

Malate synthase G

Gene

glcB

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
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 annotation

Catalytic activityi

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

Cofactori

Mg2+UniRule annotation2 Publications, Mn2+UniRule annotation2 PublicationsNote: Mg2+. Mn2+ is able to replace Mg2+.UniRule annotation2 Publications

Enzyme regulationi

By bromopyruvate, oxalate, and phosphoenolpyruvate. Malate inhibits the activity to 50% at 1 mM concentration. Glycolate inhibits only at fairly high concentrations.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 (icl)
  2. Malate synthase G (LH57_10025), Malate synthase G (glcB)
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei118 – 1181Acetyl-CoA; via carbonyl oxygen
Binding sitei275 – 2751Acetyl-CoA
Binding sitei305 – 3051Acetyl-CoA
Binding sitei312 – 3121Acetyl-CoA
Active sitei339 – 3391Proton acceptor
Binding sitei339 – 3391Glyoxylate
Metal bindingi434 – 4341Magnesium
Binding sitei434 – 4341Glyoxylate
Metal bindingi462 – 4621Magnesium
Binding sitei543 – 5431Acetyl-CoA; via carbonyl oxygen
Active sitei633 – 6331Proton donor
Binding sitei633 – 6331Acetyl-CoA

GO - Molecular functioni

  • magnesium ion binding Source: MTBBASE
  • malate synthase activity Source: MTBBASE
  • manganese ion binding Source: MTBBASE

GO - Biological processi

  • coenzyme A metabolic process Source: MTBBASE
  • glyoxylate cycle Source: MTBBASE
  • 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

UniPathwayiUPA00703; UER00720.

Names & Taxonomyi

Protein namesi
Recommended name:
Malate synthase GUniRule annotation (EC:2.3.3.9UniRule annotation)
Gene namesi
Name:glcBUniRule annotation
Ordered Locus Names:Rv1837c
ORF Names:MTCY1A11.06
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv1837c.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

  • cell wall Source: MTBBASE
  • cytosol Source: MTBBASE
  • extracellular region Source: MTBBASE
  • plasma membrane Source: MTBBASE
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 741741Malate synthase GPRO_0000166889Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei619 – 6191Cysteine sulfenic acid (-SOH)UniRule annotation

Keywords - PTMi

Oxidation

Proteomic databases

PaxDbiP9WK17.

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

STRINGi83332.Rv1837c.

Structurei

Secondary structure

1
741
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 74Combined sources
Beta strandi10 – 134Combined sources
Helixi14 – 229Combined sources
Turni26 – 294Combined sources
Helixi32 – 6938Combined sources
Beta strandi73 – 753Combined sources
Helixi78 – 8710Combined sources
Helixi107 – 1104Combined sources
Beta strandi116 – 1205Combined sources
Helixi124 – 1318Combined sources
Helixi132 – 1343Combined sources
Beta strandi135 – 1373Combined sources
Helixi138 – 1436Combined sources
Helixi162 – 17918Combined sources
Beta strandi182 – 1854Combined sources
Helixi187 – 1893Combined sources
Beta strandi192 – 1965Combined sources
Beta strandi199 – 2035Combined sources
Beta strandi211 – 2133Combined sources
Helixi214 – 2163Combined sources
Beta strandi217 – 2237Combined sources
Beta strandi226 – 2349Combined sources
Beta strandi237 – 2437Combined sources
Helixi248 – 2525Combined sources
Beta strandi257 – 2637Combined sources
Beta strandi266 – 2738Combined sources
Helixi281 – 29515Combined sources
Beta strandi300 – 3056Combined sources
Beta strandi308 – 3136Combined sources
Beta strandi318 – 3214Combined sources
Beta strandi323 – 3253Combined sources
Beta strandi327 – 3304Combined sources
Beta strandi335 – 3395Combined sources
Beta strandi346 – 3527Combined sources
Beta strandi357 – 3593Combined sources
Helixi360 – 37213Combined sources
Helixi373 – 3764Combined sources
Turni380 – 3823Combined sources
Beta strandi385 – 3873Combined sources
Beta strandi393 – 3975Combined sources
Helixi403 – 42018Combined sources
Beta strandi427 – 4337Combined sources
Helixi436 – 4394Combined sources
Helixi442 – 4487Combined sources
Turni449 – 4524Combined sources
Beta strandi453 – 4586Combined sources
Helixi460 – 47011Combined sources
Helixi472 – 4743Combined sources
Helixi480 – 4856Combined sources
Helixi487 – 50216Combined sources
Turni506 – 5083Combined sources
Beta strandi509 – 5135Combined sources
Helixi522 – 5287Combined sources
Helixi531 – 5344Combined sources
Beta strandi538 – 5447Combined sources
Helixi545 – 55713Combined sources
Helixi560 – 5678Combined sources
Helixi575 – 5784Combined sources
Helixi591 – 61525Combined sources
Beta strandi620 – 6234Combined sources
Beta strandi629 – 6324Combined sources
Helixi634 – 64916Combined sources
Helixi655 – 67218Combined sources
Turni673 – 6753Combined sources
Helixi686 – 6883Combined sources
Helixi690 – 70011Combined sources
Helixi702 – 7043Combined sources
Helixi706 – 7083Combined sources
Helixi711 – 72616Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GQ3X-ray2.30A/B1-727[»]
3S9IX-ray1.90A1-741[»]
3S9ZX-ray1.79A1-741[»]
3SADX-ray1.82A1-741[»]
3SAZX-ray2.04A1-741[»]
3SB0X-ray2.20A1-741[»]
ProteinModelPortaliP9WK17.
SMRiP9WK17. Positions 2-727.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni125 – 1295Acetyl-CoA binding
Regioni459 – 4624Glyoxylate binding
Regioni618 – 6214Acetyl-CoA binding

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4107QP3. Bacteria.
COG2225. LUCA.
KOiK01638.
OMAiPKMHGPD.
PhylomeDBiP9WK17.

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.

P9WK17-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDRVSVGNL RIARVLYDFV NNEALPGTDI DPDSFWAGVD KVVADLTPQN
60 70 80 90 100
QALLNARDEL QAQIDKWHRR RVIEPIDMDA YRQFLTEIGY LLPEPDDFTI
110 120 130 140 150
TTSGVDAEIT TTAGPQLVVP VLNARFALNA ANARWGSLYD ALYGTDVIPE
160 170 180 190 200
TDGAEKGPTY NKVRGDKVIA YARKFLDDSV PLSSGSFGDA TGFTVQDGQL
210 220 230 240 250
VVALPDKSTG LANPGQFAGY TGAAESPTSV LLINHGLHIE ILIDPESQVG
260 270 280 290 300
TTDRAGVKDV ILESAITTIM DFEDSVAAVD AADKVLGYRN WLGLNKGDLA
310 320 330 340 350
AAVDKDGTAF LRVLNRDRNY TAPGGGQFTL PGRSLMFVRN VGHLMTNDAI
360 370 380 390 400
VDTDGSEVFE GIMDALFTGL IAIHGLKASD VNGPLINSRT GSIYIVKPKM
410 420 430 440 450
HGPAEVAFTC ELFSRVEDVL GLPQNTMKIG IMDEERRTTV NLKACIKAAA
460 470 480 490 500
DRVVFINTGF LDRTGDEIHT SMEAGPMVRK GTMKSQPWIL AYEDHNVDAG
510 520 530 540 550
LAAGFSGRAQ VGKGMWTMTE LMADMVETKI AQPRAGASTA WVPSPTAATL
560 570 580 590 600
HALHYHQVDV AAVQQGLAGK RRATIEQLLT IPLAKELAWA PDEIREEVDN
610 620 630 640 650
NCQSILGYVV RWVDQGVGCS KVPDIHDVAL MEDRATLRIS SQLLANWLRH
660 670 680 690 700
GVITSADVRA SLERMAPLVD RQNAGDVAYR PMAPNFDDSI AFLAAQELIL
710 720 730 740
SGAQQPNGYT EPILHRRRRE FKARAAEKPA PSDRAGDDAA R
Length:741
Mass (Da):80,403
Last modified:April 16, 2014 - v1
Checksum:iA92F54E0FE8B7C64
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP44603.1.
PIRiF70722.
RefSeqiNP_216353.1. NC_000962.3.
WP_003409271.1. NZ_KK339370.1.

Genome annotation databases

EnsemblBacteriaiCCP44603; CCP44603; Rv1837c.
GeneIDi885713.
KEGGimtu:Rv1837c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP44603.1.
PIRiF70722.
RefSeqiNP_216353.1. NC_000962.3.
WP_003409271.1. NZ_KK339370.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GQ3X-ray2.30A/B1-727[»]
3S9IX-ray1.90A1-741[»]
3S9ZX-ray1.79A1-741[»]
3SADX-ray1.82A1-741[»]
3SAZX-ray2.04A1-741[»]
3SB0X-ray2.20A1-741[»]
ProteinModelPortaliP9WK17.
SMRiP9WK17. Positions 2-727.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv1837c.

Proteomic databases

PaxDbiP9WK17.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP44603; CCP44603; Rv1837c.
GeneIDi885713.
KEGGimtu:Rv1837c.

Organism-specific databases

TubercuListiRv1837c.

Phylogenomic databases

eggNOGiENOG4107QP3. Bacteria.
COG2225. LUCA.
KOiK01638.
OMAiPKMHGPD.
PhylomeDBiP9WK17.

Enzyme and pathway databases

UniPathwayiUPA00703; UER00720.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 25618 / H37Rv.
  2. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ATCC 25618 / H37Rv.
  3. "The product complex of M. tuberculosis malate synthase revisited."
    Anstrom D.M., Remington S.J.
    Protein Sci. 15:2002-2007(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-726 IN COMPLEX WITH SUBSTRATES AND MAGNESIUM ION, COFACTOR, SUBUNIT.
  4. "Structure-guided discovery of phenyl-diketo acids as potent inhibitors of M. tuberculosis malate synthase."
    Krieger I.V., Freundlich J.S., Gawandi V.B., Roberts J.P., Sun Q., Owen J.L., Fraile M.T., Huss S.I., Lavandera J.L., Ioerger T.R., Sacchettini J.C.
    Chem. Biol. 19:1556-1567(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND MAGNESIUM ION, ENZYME REGULATION, COFACTOR, SUBUNIT.

Entry informationi

Entry nameiMASZ_MYCTU
AccessioniPrimary (citable) accession number: P9WK17
Secondary accession number(s): L0T815, P0A5J4, Q50596
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: December 9, 2015
This is version 17 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  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.