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Protein

Malate synthase G

Gene

glcB

Organism
Geobacillus thermodenitrificans (strain NG80-2)
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 sitei117 – 1171Acetyl-CoA; via carbonyl oxygenUniRule annotation
Binding sitei275 – 2751Acetyl-CoAUniRule annotation
Binding sitei312 – 3121Acetyl-CoAUniRule annotation
Active sitei339 – 3391Proton acceptorUniRule annotation
Binding sitei339 – 3391GlyoxylateUniRule annotation
Metal bindingi431 – 4311MagnesiumUniRule annotation
Binding sitei431 – 4311GlyoxylateUniRule annotation
Metal bindingi459 – 4591MagnesiumUniRule annotation
Binding sitei540 – 5401Acetyl-CoA; via carbonyl oxygenUniRule annotation
Active sitei630 – 6301Proton 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

BioCyciGTHE420246:GIXT-1456-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:GTNG_1384
OrganismiGeobacillus thermodenitrificans (strain NG80-2)
Taxonomic identifieri420246 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus
ProteomesiUP000001578: Chromosome

Subcellular locationi

Cytoplasm 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 – 727727Malate synthase GPRO_1000056903Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei616 – 6161Cysteine sulfenic acid (-SOH)UniRule annotation

Keywords - PTMi

Oxidation

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi420246.GTNG_1384.

Structurei

3D structure databases

ProteinModelPortaliA4IN50.
SMRiA4IN50. Positions 5-723.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni124 – 1252Acetyl-CoA bindingUniRule annotation
Regioni456 – 4594Glyoxylate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG2225.
HOGENOMiHOG000220740.
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.

A4IN50-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIEYVQAGTI QVAKVLYEFV NEELLPNSGL DQDKFWSDFA ALIADLTPRN
60 70 80 90 100
KELLARRDEI QEKLNEWYKE HRGRFDFHEY KAFLTDIGYL EPEVEDFEIT
110 120 130 140 150
TDNVDEEIAV QAGPQLVVPL TNARYALNAA NARWGSLYDA LYGTDAISEE
160 170 180 190 200
DGAERGSSYN PVRGAKVIAY GRQFLDEAVP LVEHSHKDAV QYAIVDGKLV
210 220 230 240 250
VTTEGGATTG LKEPEKLIGF QGEPQNPTAV LLKNNGLHIE IQIDREHPVG
260 270 280 290 300
KTDKAGIKDI VLEAAVTTIM DGEDSVAAVD AEDKVVVYRN LFGLIKGDLT
310 320 330 340 350
ATFEKNGKRL TRTLNPDREY KTPDGGELVL PGRSLMFVRN VGHLMTNNAI
360 370 380 390 400
LDANGEEVYE GIIDAVVTSL IMKHSLIGNT RYLNSRKGSI YIVKPKMHGS
410 420 430 440 450
AEVAFANELF DRVEDMLGLE RNTIKIGVMD EERRTSLNLK NCIYEVRDRI
460 470 480 490 500
VFINTGFLDR TGDEIHTSME AGPMRRKNDM KSSTWLAGYE KSNVAVGLAA
510 520 530 540 550
GFRGRAQIGK GMWAMPDLMA EMLKQKGAQL KAGANTAWVP SPTAATLHAL
560 570 580 590 600
HYHQVNVAAV QNELANDRND YRDDILQIPV VDNPQWTADE IQEELDNNCQ
610 620 630 640 650
SILGYVVRWI DQGIGCSKVP DIHNIGLMED RATLRISSQI LANWLHHGIC
660 670 680 690 700
TKEQVLETFK RMAKVVDEQN AGDPNYRPMA PNYDDSVAFQ AACDLVFLGY
710 720
EQPNGYTEPI LHRRRQEAKA KFAAVQQ
Length:727
Mass (Da):81,200
Last modified:May 1, 2007 - v1
Checksum:i37B1B2D489B3ADA2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000557 Genomic DNA. Translation: ABO66754.1.
RefSeqiYP_001125499.1. NC_009328.1.

Genome annotation databases

EnsemblBacteriaiABO66754; ABO66754; GTNG_1384.
GeneIDi4966323.
KEGGigtn:GTNG_1384.
PATRICi21979151. VBIGeoThe136879_1455.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000557 Genomic DNA. Translation: ABO66754.1.
RefSeqiYP_001125499.1. NC_009328.1.

3D structure databases

ProteinModelPortaliA4IN50.
SMRiA4IN50. Positions 5-723.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi420246.GTNG_1384.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABO66754; ABO66754; GTNG_1384.
GeneIDi4966323.
KEGGigtn:GTNG_1384.
PATRICi21979151. VBIGeoThe136879_1455.

Phylogenomic databases

eggNOGiCOG2225.
HOGENOMiHOG000220740.
KOiK01638.
OMAiPKMHGPD.
OrthoDBiEOG6HJ286.

Enzyme and pathway databases

UniPathwayiUPA00703; UER00720.
BioCyciGTHE420246:GIXT-1456-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

  1. "Genome and proteome of long-chain alkane degrading Geobacillus thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir."
    Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X., Han W., Peng X., Liu R., Wang L.
    Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NG80-2.

Entry informationi

Entry nameiMASZ_GEOTN
AccessioniPrimary (citable) accession number: A4IN50
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 1, 2007
Last modified: January 7, 2015
This is version 54 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

Complete proteome

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.