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Q05509

- GLME_CLOTT

UniProt

Q05509 - GLME_CLOTT

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Protein

Glutamate mutase epsilon subunit

Gene

glmE

Organism
Clostridium tetanomorphum
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the carbon skeleton rearrangement of L-glutamate to L-threo-3-methylaspartate ((2S,3S)-3-methylaspartate).1 PublicationUniRule annotation

Catalytic activityi

L-threo-3-methylaspartate = L-glutamate.1 PublicationUniRule annotation

Cofactori

adenosylcob(III)alamin1 PublicationUniRule annotation

Kineticsi

Kcat is 20.6 sec(-1) for mutase activity with L-glutamate.

  1. KM=18 µM for adenosylcobalamin1 Publication
  2. KM=1.09 mM for L-glutamate1 Publication

Vmax=22.8 µmol/min/mg enzyme1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei66 – 661L-glutamateUniRule annotation
Binding sitei68 – 681Adenosylcobalamin; via carbonyl oxygenUniRule annotation
Binding sitei100 – 1001L-glutamateUniRule annotation
Binding sitei123 – 1231AdenosylcobalaminUniRule annotation
Binding sitei171 – 1711L-glutamateUniRule annotation
Binding sitei177 – 1771L-glutamateUniRule annotation
Binding sitei180 – 1801Adenosylcobalamin; via carbonyl oxygenUniRule annotation
Binding sitei181 – 1811L-glutamateUniRule annotation
Binding sitei297 – 2971Adenosylcobalamin; via amide nitrogenUniRule annotation
Binding sitei326 – 3261AdenosylcobalaminUniRule annotation
Binding sitei330 – 3301Adenosylcobalamin; via carbonyl oxygenUniRule annotation
Binding sitei334 – 3341Adenosylcobalamin; via amide nitrogenUniRule annotation

GO - Molecular functioni

  1. cobalamin binding Source: UniProtKB-KW
  2. methylaspartate mutase activity Source: UniProtKB-EC

GO - Biological processi

  1. anaerobic glutamate catabolic process Source: InterPro
  2. glutamate catabolic process via L-citramalate Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Ligandi

Cobalamin, Cobalt

Enzyme and pathway databases

SABIO-RKQ05509.
UniPathwayiUPA00561; UER00617.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate mutase epsilon subunitUniRule annotation (EC:5.4.99.1UniRule annotation)
Alternative name(s):
Glutamate mutase E chainUniRule annotation
Glutamate mutase large subunitUniRule annotation
Methylaspartate mutaseUniRule annotation
Gene namesi
Name:glmEUniRule annotation
Synonyms:mutE
OrganismiClostridium tetanomorphum
Taxonomic identifieri1553 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 485485Glutamate mutase epsilon subunitPRO_0000087512Add
BLAST

Interactioni

Subunit structurei

Heterotetramer composed of 2 epsilon subunits (GlmE) and 2 sigma subunits (GlmS). GlmE exists as a homodimer and GlmS as a monomer (Probable).1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ05509.
SMRiQ05509. Positions 1-483.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni149 – 1502L-glutamate bindingUniRule annotation

Sequence similaritiesi

Belongs to the methylaspartate mutase GlmE subunit family.UniRule annotation

Family and domain databases

Gene3Di3.20.20.240. 1 hit.
3.90.970.10. 1 hit.
HAMAPiMF_01923. Me_Asp_mutase_E.
InterProiIPR016176. Cbl-dep_enz_cat.
IPR014348. Cbl-dep_enz_cat-sub.
IPR006396. Glu_mut_E.
IPR014714. Glu_mut_E_C_dom.
[Graphical view]
PfamiPF06368. Met_asp_mut_E. 1 hit.
[Graphical view]
PIRSFiPIRSF001495. Met_asp_mut_epsi. 1 hit.
SUPFAMiSSF51703. SSF51703. 1 hit.
TIGRFAMsiTIGR01503. MthylAspMut_E. 1 hit.

Sequencei

Sequence statusi: Complete.

Q05509-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MELKNKKWTD EEFFKQREEV LKQWPTGKEV DLQEAVDYLK KVPTEKNFAD
60 70 80 90 100
KLVRAKEAGI TLAQPRAGVA LLDEHINLLR YLQDEGGADL LPSTIDAYTR
110 120 130 140 150
QNRYEECEIG IKESEKAGRS LLNGFPGVNH GVKGCRKVLE SVNLPLQARH
160 170 180 190 200
GTPDSRLLAE IIHAGGWTSN EGGGISYNIP YAKSVPIDKC LKDWQYCDRL
210 220 230 240 250
VGFYEEQGVH INREPFGPLT GTLVPPSMSN AVGITEALLA AEQGVKNITV
260 270 280 290 300
GYGECGNMLQ DIAALRCLEE QTNEYLKAYG YNDVFVTTVF HQWMGGFPQD
310 320 330 340 350
ESKAFGVIVT ATTIASLAGA TKVIVKTPHE AIGIPTKEAN ASGIKATKMA
360 370 380 390 400
LNMLEGQRMP MSKELETEMA IIKAETKCIL DKMFELGKGD LAVGTVKAFE
410 420 430 440 450
TGVMDIPFGP SKYNAGKMMP VRDNLGCVRY LEFGNVPFTE ELKNYNRERL
460 470 480
AERAKFEGRE VSFQMVIDDI FAVGKGRLIG RPENK
Length:485
Mass (Da):53,741
Last modified:February 1, 1995 - v1
Checksum:i131792A392CACCC0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 81W → L AA sequence (PubMed:1397267)Curated
Sequence conflicti12 – 121E → G AA sequence (PubMed:1397267)Curated
Sequence conflicti17 – 171R → A AA sequence (PubMed:1397267)Curated
Sequence conflicti19 – 191E → G AA sequence (PubMed:1397267)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70499 Genomic DNA. Translation: CAA49910.1.
X70695 Genomic DNA. Translation: CAA50026.1.
S48141 Genomic DNA. Translation: AAB24069.1.
PIRiS32433.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70499 Genomic DNA. Translation: CAA49910.1 .
X70695 Genomic DNA. Translation: CAA50026.1 .
S48141 Genomic DNA. Translation: AAB24069.1 .
PIRi S32433.

3D structure databases

ProteinModelPortali Q05509.
SMRi Q05509. Positions 1-483.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00561 ; UER00617 .
SABIO-RK Q05509.

Family and domain databases

Gene3Di 3.20.20.240. 1 hit.
3.90.970.10. 1 hit.
HAMAPi MF_01923. Me_Asp_mutase_E.
InterProi IPR016176. Cbl-dep_enz_cat.
IPR014348. Cbl-dep_enz_cat-sub.
IPR006396. Glu_mut_E.
IPR014714. Glu_mut_E_C_dom.
[Graphical view ]
Pfami PF06368. Met_asp_mut_E. 1 hit.
[Graphical view ]
PIRSFi PIRSF001495. Met_asp_mut_epsi. 1 hit.
SUPFAMi SSF51703. SSF51703. 1 hit.
TIGRFAMsi TIGR01503. MthylAspMut_E. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Cloning and sequencing of glutamate mutase component E from Clostridium tetanomorphum. Organization of the mut genes."
    Holloway D.E., Marsh E.N.G.
    FEBS Lett. 317:44-48(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: NCIMB 11547.
  2. "Cloning and sequencing of glutamate mutase component E from Clostridium tetanomorphum."
    Brecht M., Kellermann J., Plueckthun A.
    FEBS Lett. 319:84-89(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    Strain: ATCC 15920 / DSM 528 / H1.
  3. "Cloning, sequencing, and expression in Escherichia coli of the Clostridium tetanomorphum gene encoding beta-methylaspartase and characterization of the recombinant protein."
    Goda S.K., Minton N.P., Botting N.P., Gani D.
    Biochemistry 31:10747-10756(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 278-485.
    Strain: ATCC 15920 / DSM 528 / H1.
  4. "Cloning and sequencing of glutamate mutase component S from Clostridium tetanomorphum. Homologies with other cobalamin-dependent enzymes."
    Marsh E.N.G., Holloway D.E.
    FEBS Lett. 310:167-170(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-20.
    Strain: NCIMB 11547.
  5. "Adenosylcobalamin-dependent glutamate mutase from Clostridium tetanomorphum. Overexpression in Escherichia coli, purification, and characterization of the recombinant enzyme."
    Holloway D.E., Marsh E.N.
    J. Biol. Chem. 269:20425-20430(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT.

Entry informationi

Entry nameiGLME_CLOTT
AccessioniPrimary (citable) accession number: Q05509
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 26, 2014
This is version 72 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

Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3