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B8ZSN3

- MASZ_MYCLB

UniProt

B8ZSN3 - MASZ_MYCLB

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Protein
Malate synthase G
Gene
glcB, MLBr02069
Organism
Mycobacterium leprae (strain Br4923)
Status
Reviewed - 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 By similarity.UniRule annotation

Catalytic activityi

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

Cofactori

Magnesium.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei118 – 1181Acetyl-CoA; via carbonyl oxygen By similarity
Binding sitei276 – 2761Acetyl-CoA By similarity
Binding sitei313 – 3131Acetyl-CoA By similarity
Active sitei340 – 3401Proton acceptor By similarity
Binding sitei340 – 3401Glyoxylate By similarity
Metal bindingi439 – 4391Magnesium
Binding sitei439 – 4391Glyoxylate By similarity
Metal bindingi467 – 4671Magnesium
Binding sitei548 – 5481Acetyl-CoA; via carbonyl oxygen By similarity
Active sitei638 – 6381Proton donor By similarity

GO - Molecular functioni

  1. malate synthase activity Source: UniProtKB-HAMAP
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. glyoxylate cycle Source: UniProtKB-HAMAP
  2. 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

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

Names & Taxonomyi

Protein namesi
Recommended name:
Malate synthase G (EC:2.3.3.9)
Gene namesi
Name:glcB
Ordered Locus Names:MLBr02069
OrganismiMycobacterium leprae (strain Br4923)
Taxonomic identifieri561304 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium
ProteomesiUP000006900: Chromosome

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 731731Malate synthase GUniRule annotation
PRO_1000147426Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Oxidation

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi561304.MLBr_02069.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4EX4X-ray2.10A/B1-731[»]

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni125 – 1262Acetyl-CoA binding By similarity
Regioni464 – 4674Glyoxylate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2225.
KOiK01638.
OMAiSTIMDFE.
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

MTDRVSAGNL RVARVLYDFV NNEALPGTDI NPNSFWSGVA KVVADLTPQN    50
QSLLNSRDEL QAQIDKWHRH RVIEPFDVDA YRQFLIDIGY LLPEPDDFTI 100
STSGVDDEIT MTAGPQLVVP VLNARFALNA ANARWGSLYD ALYGTDTIPE 150
TEGAEKGSEY NKIRGDKVIA YARKFMDQAV PLASDSWTNA TGVSIFDGQL 200
QIAIGTNSTG LASPEKFVGY NRQLRSSNWS VLLANHGLHI EVLIDPESPI 250
GKTDPVGIKD VILESAITTI MDFEDSVTAV DADDKVRGYR NWLGLNKGDL 300
TEEVNKDGKT FTRVLNADRS YTTPDGGELT LPGRSLLFVR NVGHLTTSDA 350
ILVDGGDGQE KEVFEGIIDA VFTGLAAIHG LKTGEANGPL TNSRTGSIYI 400
VKPKMHGPAE VAFTCELFSR VEDVLGLPQG TLKVGIMDEE RRTTLNLKAC 450
IKAAADRVVF INTGFLDRTG DEIHTSMEAG PMIRKGAMKN STWIKAYEDA 500
NVDIGLAAGF KGKAQIGKGM WAMTELMADM VEQKIGQPKA GATTAWVPSP 550
TAATLHAMHY HQVDVAAVQQ ELTGQRRATV DQLLTIPLAK ELAWAPEEIR 600
EEVDNDCQSI LGYVVRWVDQ GIGCSKVPDI HNVALMEDRA TLRISSQLLA 650
NWLRHGVITS EDVRASLERM APLVDQQNAE DPAYRPMAPN FDDSIAFLAA 700
QELILSGAQQ PNGYTEPILH RRRREFKAQN R 731
Length:731
Mass (Da):80,143
Last modified:March 3, 2009 - v1
Checksum:i3878C0DAE26DECDA
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
FM211192 Genomic DNA. Translation: CAR72166.1.
RefSeqiYP_002504009.1. NC_011896.1.

Genome annotation databases

EnsemblBacteriaiCAR72166; CAR72166; MLBr02069.
GeneIDi7325139.
KEGGimlb:MLBr_02069.
PATRICi18047419. VBIMycLep121698_3918.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
FM211192 Genomic DNA. Translation: CAR72166.1 .
RefSeqi YP_002504009.1. NC_011896.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4EX4 X-ray 2.10 A/B 1-731 [» ]
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 561304.MLBr_02069.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAR72166 ; CAR72166 ; MLBr02069 .
GeneIDi 7325139.
KEGGi mlb:MLBr_02069.
PATRICi 18047419. VBIMycLep121698_3918.

Phylogenomic databases

eggNOGi COG2225.
KOi K01638.
OMAi STIMDFE.
OrthoDBi EOG6HJ286.

Enzyme and pathway databases

UniPathwayi UPA00703 ; UER00720 .
BioCyci MLEP561304:GJP6-2112-MONOMER.

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. 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: September 3, 2014
This is version 38 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

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

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