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 leprae (strain Br4923)
Status
Reviewed-Annotation score: Annotation score: 4 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

Pathway:iglyoxylate 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. no protein annotated in this organism
  2. 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 oxygenUniRule annotation
Binding sitei276 – 2761Acetyl-CoAUniRule annotation
Binding sitei313 – 3131Acetyl-CoAUniRule annotation
Active sitei340 – 3401Proton acceptorUniRule annotation
Binding sitei340 – 3401GlyoxylateUniRule annotation
Metal bindingi439 – 4391Magnesium
Binding sitei439 – 4391GlyoxylateUniRule annotation
Metal bindingi467 – 4671Magnesium
Binding sitei548 – 5481Acetyl-CoA; via carbonyl oxygenUniRule annotation
Active sitei638 – 6381Proton donorUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Glyoxylate bypass, Tricarboxylic acid cycle

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMLEP561304:GJP6-2112-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:MLBr02069
OrganismiMycobacterium leprae (strain Br4923)
Taxonomic identifieri561304 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 731731Malate synthase GPRO_1000147426Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei624 – 6241Cysteine sulfenic acid (-SOH)UniRule annotation

Keywords - PTMi

Oxidation

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1
731
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 74Combined sources
Beta strandi10 – 134Combined sources
Helixi14 – 2310Combined sources
Helixi32 – 7039Combined sources
Helixi78 – 8710Combined sources
Helixi107 – 1104Combined sources
Beta strandi116 – 1205Combined sources
Helixi124 – 1329Combined sources
Beta strandi135 – 1373Combined sources
Helixi138 – 1436Combined sources
Helixi162 – 17918Combined sources
Helixi187 – 1893Combined sources
Beta strandi207 – 2093Combined sources
Helixi214 – 2163Combined sources
Beta strandi217 – 2204Combined sources
Beta strandi232 – 2354Combined sources
Beta strandi238 – 2436Combined sources
Helixi251 – 2533Combined sources
Beta strandi260 – 2645Combined sources
Beta strandi267 – 2748Combined sources
Helixi282 – 29716Combined sources
Beta strandi302 – 3065Combined sources
Beta strandi309 – 3135Combined sources
Beta strandi319 – 3224Combined sources
Beta strandi328 – 3314Combined sources
Beta strandi336 – 3405Combined sources
Beta strandi347 – 3537Combined sources
Beta strandi359 – 3646Combined sources
Helixi365 – 37713Combined sources
Helixi378 – 3803Combined sources
Helixi385 – 3873Combined sources
Beta strandi394 – 3963Combined sources
Beta strandi398 – 4025Combined sources
Helixi408 – 42518Combined sources
Beta strandi432 – 4387Combined sources
Helixi441 – 4444Combined sources
Helixi447 – 4537Combined sources
Turni454 – 4574Combined sources
Beta strandi458 – 4636Combined sources
Helixi465 – 47511Combined sources
Helixi477 – 4793Combined sources
Turni485 – 4873Combined sources
Helixi488 – 4903Combined sources
Helixi492 – 50716Combined sources
Turni511 – 5133Combined sources
Beta strandi514 – 5185Combined sources
Beta strandi523 – 5253Combined sources
Helixi527 – 5337Combined sources
Helixi536 – 5394Combined sources
Beta strandi543 – 5497Combined sources
Helixi550 – 56213Combined sources
Helixi565 – 5728Combined sources
Helixi580 – 5834Combined sources
Helixi596 – 62025Combined sources
Beta strandi625 – 6284Combined sources
Beta strandi634 – 6374Combined sources
Helixi639 – 65416Combined sources
Helixi660 – 67718Combined sources
Turni678 – 6803Combined sources
Helixi691 – 6933Combined sources
Helixi695 – 70511Combined sources
Helixi707 – 7093Combined sources
Helixi711 – 7133Combined sources
Helixi716 – 72813Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4EX4X-ray2.10A/B1-731[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni125 – 1262Acetyl-CoA bindingUniRule annotation
Regioni464 – 4674Glyoxylate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG2225.
KOiK01638.
OMAiPKMHGPD.
OrthoDBiEOG6HJ286.

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.

B8ZSN3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDRVSAGNL RVARVLYDFV NNEALPGTDI NPNSFWSGVA KVVADLTPQN
60 70 80 90 100
QSLLNSRDEL QAQIDKWHRH RVIEPFDVDA YRQFLIDIGY LLPEPDDFTI
110 120 130 140 150
STSGVDDEIT MTAGPQLVVP VLNARFALNA ANARWGSLYD ALYGTDTIPE
160 170 180 190 200
TEGAEKGSEY NKIRGDKVIA YARKFMDQAV PLASDSWTNA TGVSIFDGQL
210 220 230 240 250
QIAIGTNSTG LASPEKFVGY NRQLRSSNWS VLLANHGLHI EVLIDPESPI
260 270 280 290 300
GKTDPVGIKD VILESAITTI MDFEDSVTAV DADDKVRGYR NWLGLNKGDL
310 320 330 340 350
TEEVNKDGKT FTRVLNADRS YTTPDGGELT LPGRSLLFVR NVGHLTTSDA
360 370 380 390 400
ILVDGGDGQE KEVFEGIIDA VFTGLAAIHG LKTGEANGPL TNSRTGSIYI
410 420 430 440 450
VKPKMHGPAE VAFTCELFSR VEDVLGLPQG TLKVGIMDEE RRTTLNLKAC
460 470 480 490 500
IKAAADRVVF INTGFLDRTG DEIHTSMEAG PMIRKGAMKN STWIKAYEDA
510 520 530 540 550
NVDIGLAAGF KGKAQIGKGM WAMTELMADM VEQKIGQPKA GATTAWVPSP
560 570 580 590 600
TAATLHAMHY HQVDVAAVQQ ELTGQRRATV DQLLTIPLAK ELAWAPEEIR
610 620 630 640 650
EEVDNDCQSI LGYVVRWVDQ GIGCSKVPDI HNVALMEDRA TLRISSQLLA
660 670 680 690 700
NWLRHGVITS EDVRASLERM APLVDQQNAE DPAYRPMAPN FDDSIAFLAA
710 720 730
QELILSGAQQ PNGYTEPILH RRRREFKAQN R
Length:731
Mass (Da):80,143
Last modified:March 3, 2009 - v1
Checksum:i3878C0DAE26DECDA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FM211192 Genomic DNA. Translation: CAR72166.1.
RefSeqiWP_012634443.1. NC_011896.1.

Genome annotation databases

EnsemblBacteriaiCAR72166; CAR72166; MLBr02069.
KEGGimlb:MLBr_02069.
PATRICi18047419. VBIMycLep121698_3918.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FM211192 Genomic DNA. Translation: CAR72166.1.
RefSeqiWP_012634443.1. NC_011896.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4EX4X-ray2.10A/B1-731[»]
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAR72166; CAR72166; MLBr02069.
KEGGimlb:MLBr_02069.
PATRICi18047419. VBIMycLep121698_3918.

Phylogenomic databases

eggNOGiCOG2225.
KOiK01638.
OMAiPKMHGPD.
OrthoDBiEOG6HJ286.

Enzyme and pathway databases

UniPathwayiUPA00703; UER00720.
BioCyciMLEP561304:GJP6-2112-MONOMER.

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: Br4923.
  2. "The structure of glcb from mycobacterium leprae."
    Seattle structural genomics center for infectious disease (SSGCID)
    Submitted (APR-2012) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH MAGNESIUM ION, SUBUNIT.

Entry informationi

Entry nameiMASZ_MYCLB
AccessioniPrimary (citable) accession number: B8ZSN3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: July 22, 2015
This is version 48 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.