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Protein

Malate synthase G

Gene

glcB

Organism
Rhodococcus fascians
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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 annotation

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 bindingi432 – 4321MagnesiumUniRule annotation
Binding sitei432 – 4321GlyoxylateUniRule annotation
Metal bindingi460 – 4601MagnesiumUniRule annotation
Binding sitei541 – 5411Acetyl-CoA; via carbonyl oxygenUniRule annotation
Active sitei631 – 6311Proton 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

UniPathwayiUPA00703; UER00720.

Names & Taxonomyi

Protein namesi
Recommended name:
Malate synthase GUniRule annotation (EC:2.3.3.9UniRule annotation)
Gene namesi
Name:glcBUniRule annotation
Synonyms:vicA
OrganismiRhodococcus fascians
Taxonomic identifieri1828 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeNocardiaceaeRhodococcus

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 – 724724Malate synthase GPRO_0000166899Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei617 – 6171Cysteine sulfenic acid (-SOH)UniRule annotation

Keywords - PTMi

Oxidation

Interactioni

Subunit structurei

Monomer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ9AE55.
SMRiQ9AE55. Positions 2-721.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni125 – 1262Acetyl-CoA bindingUniRule annotation
Regioni457 – 4604Glyoxylate bindingUniRule annotation

Sequence similaritiesi

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

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.

Q9AE55-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDRVQAGGL QVAKVLFDFV EKEALPGTDL DSEAFWAGAA SVIADLAPKN
60 70 80 90 100
KALLAVRDEI QGKVDAWHGE HAGAEYDRAA YKAFLKEIGY LLDEPADFQI
110 120 130 140 150
HTSGVDTEIT TTAGPQLVVP VLNARFAINA SNARWGSLYD ALYGTDAIPE
160 170 180 190 200
TDGAEKGTSY NKVRGDKVIA FARDFLDEAL PLSSGSHVGT TGYVVDAASL
210 220 230 240 250
TVTLADGSTV GLKDPSQLLG YQGTPDAPTA ILFVHNGLHF EIQIDPESPI
260 270 280 290 300
GKTDGAGVKD VLLESAVTTI MDFEDSVAAV DADDKVLGYR NWLGLMKGDL
310 320 330 340 350
TEEVSKGGKT FTRAMNKDRT YTSVDGSELT LHGRSLLFVR NVGHLMTSDA
360 370 380 390 400
ILDADGNEVP EGILDALFTS LAGLHSLTPD NVLSNSRTGS LYIVKPKMHG
410 420 430 440 450
PDEVAFTAEL FGRVEQVLGL PTNTLKVGIM DEERRTTVNL KACIQAASER
460 470 480 490 500
VVFINTGFLD RTGDEIHTSM EAGPVVRKGA MKGEKWIAAY EDFNVDTGLA
510 520 530 540 550
AGLQGKAQIG KGMWAMPDLM HDMLEQKIGH PKAGANTAWV PSPTAATLHA
560 570 580 590 600
LHYHKVDVFA RQHEIAKAKR ATVDEILEIP LAPSTDWTDE EKQNELDNNS
610 620 630 640 650
QSILGYVVRW IDHGVGCSKV PDINDIALME DRATLRISSQ FIANWLRHGI
660 670 680 690 700
VTEEQVRESL KRMAPVVDRQ NASDPTYKPL APDFDTNIAF QAASDLIFQG
710 720
TSQPNGYTEP ILHRRRREYK AVNA
Length:724
Mass (Da):78,610
Last modified:June 1, 2001 - v1
Checksum:iF889FE883890995E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ301559 Genomic DNA. Translation: CAC35701.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ301559 Genomic DNA. Translation: CAC35701.1.

3D structure databases

ProteinModelPortaliQ9AE55.
SMRiQ9AE55. Positions 2-721.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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

  1. "Characterization of a chromosomal locus that affects pathogenicity in Rhodococcus fascians."
    Vereecke D.M., Cornelis K., Van Montagu M., El Jaziri M., Holsters M., Goethals K.
    Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: D188.

Entry informationi

Entry nameiMASZ_RHOFA
AccessioniPrimary (citable) accession number: Q9AE55
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: June 1, 2001
Last modified: January 7, 2015
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.