Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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 (glcB), 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)DescriptionActionsGraphical viewLength
Binding sitei118Acetyl-CoA; via carbonyl oxygen1
Binding sitei275Acetyl-CoA1
Binding sitei305Acetyl-CoA1
Binding sitei312Acetyl-CoA1
Active sitei339Proton acceptor1
Binding sitei339Glyoxylate1
Metal bindingi434Magnesium1
Binding sitei434Glyoxylate1
Metal bindingi462Magnesium1
Binding sitei543Acetyl-CoA; via carbonyl oxygen1
Active sitei633Proton donor1
Binding sitei633Acetyl-CoA1

GO - Molecular functioni

  • magnesium ion binding Source: MTBBASE
  • malate synthase activity Source: UniProtKB-HAMAP

GO - Biological processi

  • coenzyme A metabolic process Source: MTBBASE
  • glyoxylate cycle Source: UniProtKB-HAMAP
  • 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

BioCyciMTBH37RV:G185E-6032-MONOMER.
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)DescriptionActionsGraphical viewLength
ChainiPRO_00001668891 – 741Malate synthase GAdd BLAST741

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei619Cysteine sulfenic acid (-SOH)UniRule annotation1

Keywords - PTMi

Oxidation

Proteomic databases

PaxDbiP9WK17.

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

STRINGi83332.Rv1837c.

Structurei

Secondary structure

1741
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 7Combined sources4
Beta strandi10 – 13Combined sources4
Helixi14 – 22Combined sources9
Turni26 – 29Combined sources4
Helixi32 – 69Combined sources38
Beta strandi73 – 75Combined 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 strandi151 – 153Combined sources3
Helixi162 – 179Combined sources18
Beta strandi182 – 185Combined sources4
Helixi187 – 189Combined sources3
Beta strandi192 – 196Combined sources5
Beta strandi199 – 203Combined sources5
Beta strandi205 – 207Combined sources3
Beta strandi211 – 213Combined sources3
Helixi214 – 216Combined sources3
Beta strandi217 – 223Combined sources7
Beta strandi226 – 234Combined sources9
Beta strandi237 – 243Combined sources7
Helixi248 – 252Combined sources5
Beta strandi257 – 263Combined sources7
Beta strandi266 – 273Combined sources8
Helixi281 – 295Combined sources15
Beta strandi300 – 305Combined sources6
Beta strandi308 – 313Combined sources6
Beta strandi318 – 321Combined sources4
Beta strandi323 – 325Combined sources3
Beta strandi327 – 330Combined sources4
Beta strandi335 – 339Combined sources5
Beta strandi346 – 352Combined sources7
Beta strandi357 – 359Combined sources3
Helixi360 – 372Combined sources13
Helixi373 – 376Combined sources4
Turni380 – 382Combined sources3
Beta strandi385 – 387Combined sources3
Beta strandi389 – 391Combined sources3
Beta strandi393 – 397Combined sources5
Helixi403 – 420Combined sources18
Beta strandi427 – 433Combined sources7
Helixi436 – 439Combined sources4
Helixi442 – 448Combined sources7
Turni449 – 452Combined sources4
Beta strandi453 – 458Combined sources6
Helixi460 – 470Combined sources11
Helixi472 – 474Combined sources3
Helixi480 – 485Combined sources6
Helixi487 – 502Combined sources16
Turni506 – 508Combined sources3
Beta strandi509 – 513Combined sources5
Helixi522 – 528Combined sources7
Helixi531 – 534Combined sources4
Beta strandi538 – 544Combined sources7
Helixi545 – 557Combined sources13
Helixi560 – 567Combined sources8
Helixi575 – 578Combined sources4
Helixi591 – 615Combined sources25
Beta strandi620 – 623Combined sources4
Beta strandi629 – 632Combined sources4
Helixi634 – 649Combined sources16
Helixi655 – 672Combined sources18
Turni673 – 675Combined sources3
Helixi686 – 688Combined sources3
Helixi690 – 700Combined sources11
Helixi702 – 704Combined sources3
Helixi706 – 708Combined sources3
Helixi711 – 726Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5C7VX-ray2.50A1-741[»]
5C9RX-ray2.00A1-741[»]
5C9TX-ray2.04A1-741[»]
5C9UX-ray1.95A1-741[»]
5C9WX-ray2.09A1-741[»]
5C9XX-ray2.10A1-741[»]
5CAHX-ray2.30A1-741[»]
5CAKX-ray1.99A1-741[»]
5CBBX-ray2.01A1-741[»]
5CBIX-ray1.99A1-741[»]
5CBJX-ray1.96A1-741[»]
5CC3X-ray2.20A1-741[»]
5CC5X-ray2.14A1-741[»]
5CC6X-ray2.10A1-741[»]
5CC7X-ray2.12A1-741[»]
5CCZX-ray2.14A1-741[»]
5CEWX-ray2.03A1-741[»]
5CJMX-ray2.13A1-741[»]
5CJNX-ray2.19A1-741[»]
5DRCX-ray2.18A1-741[»]
5DRIX-ray2.80A1-741[»]
5DX7X-ray2.10A1-741[»]
ProteinModelPortaliP9WK17.
SMRiP9WK17.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni125 – 129Acetyl-CoA binding5
Regioni459 – 462Glyoxylate binding4
Regioni618 – 621Acetyl-CoA binding4

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4107QP3. Bacteria.
COG2225. LUCA.
KOiK01638.
OMAiTEPVLHA.
PhylomeDBiP9WK17.

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.

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
PDB 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[»]
5C7VX-ray2.50A1-741[»]
5C9RX-ray2.00A1-741[»]
5C9TX-ray2.04A1-741[»]
5C9UX-ray1.95A1-741[»]
5C9WX-ray2.09A1-741[»]
5C9XX-ray2.10A1-741[»]
5CAHX-ray2.30A1-741[»]
5CAKX-ray1.99A1-741[»]
5CBBX-ray2.01A1-741[»]
5CBIX-ray1.99A1-741[»]
5CBJX-ray1.96A1-741[»]
5CC3X-ray2.20A1-741[»]
5CC5X-ray2.14A1-741[»]
5CC6X-ray2.10A1-741[»]
5CC7X-ray2.12A1-741[»]
5CCZX-ray2.14A1-741[»]
5CEWX-ray2.03A1-741[»]
5CJMX-ray2.13A1-741[»]
5CJNX-ray2.19A1-741[»]
5DRCX-ray2.18A1-741[»]
5DRIX-ray2.80A1-741[»]
5DX7X-ray2.10A1-741[»]
ProteinModelPortaliP9WK17.
SMRiP9WK17.
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.
OMAiTEPVLHA.
PhylomeDBiP9WK17.

Enzyme and pathway databases

UniPathwayiUPA00703; UER00720.
BioCyciMTBH37RV:G185E-6032-MONOMER.

Miscellaneous databases

PROiP9WK17.

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_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: November 30, 2016
This is version 22 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.