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B8ZSN3

- MASZ_MYCLB

UniProt

B8ZSN3 - MASZ_MYCLB

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Protein

Malate synthase G

Gene

glcB

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.UniRule annotation

Catalytic activityi

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

Cofactori

Pathwayi

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

  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 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 lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium
ProteomesiUP000006900: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
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

Protein-protein interaction databases

STRINGi561304.MLBr_02069.

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
Helixi214 – 2163Combined sources
Beta strandi217 – 2204Combined sources
Beta strandi232 – 2354Combined sources
Beta strandi238 – 2436Combined 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.
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

        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.
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:
EMBLi
GenBanki
DDBJi
Links Updated
FM211192 Genomic DNA. Translation: CAR72166.1 .
RefSeqi YP_002504009.1. NC_011896.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 41 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