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Q05509

- GLME_CLOTT

UniProt

Q05509 - GLME_CLOTT

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Protein
Glutamate mutase epsilon subunit
Gene
glmE, mutE
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 Publication

Catalytic activityi

L-threo-3-methylaspartate = L-glutamate.1 Publication

Cofactori

Adenosylcobalamin.1 Publication

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-glutamate

Vmax=22.8 µmol/min/mg enzyme

Pathwayi

Sites

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

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 subunit (EC:5.4.99.1)
Alternative name(s):
Glutamate mutase E chain
Glutamate mutase large subunit
Methylaspartate mutase
Gene namesi
Name:glmE
Synonyms:mutE
OrganismiClostridium tetanomorphum
Taxonomic identifieri1553 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 485485Glutamate mutase epsilon subunitUniRule annotation
PRO_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 Inferred.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ05509.
SMRiQ05509. Positions 1-483.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni149 – 1502L-glutamate binding By similarity

Sequence similaritiesi

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

MELKNKKWTD EEFFKQREEV LKQWPTGKEV DLQEAVDYLK KVPTEKNFAD    50
KLVRAKEAGI TLAQPRAGVA LLDEHINLLR YLQDEGGADL LPSTIDAYTR 100
QNRYEECEIG IKESEKAGRS LLNGFPGVNH GVKGCRKVLE SVNLPLQARH 150
GTPDSRLLAE IIHAGGWTSN EGGGISYNIP YAKSVPIDKC LKDWQYCDRL 200
VGFYEEQGVH INREPFGPLT GTLVPPSMSN AVGITEALLA AEQGVKNITV 250
GYGECGNMLQ DIAALRCLEE QTNEYLKAYG YNDVFVTTVF HQWMGGFPQD 300
ESKAFGVIVT ATTIASLAGA TKVIVKTPHE AIGIPTKEAN ASGIKATKMA 350
LNMLEGQRMP MSKELETEMA IIKAETKCIL DKMFELGKGD LAVGTVKAFE 400
TGVMDIPFGP SKYNAGKMMP VRDNLGCVRY LEFGNVPFTE ELKNYNRERL 450
AERAKFEGRE VSFQMVIDDI FAVGKGRLIG RPENK 485
Length:485
Mass (Da):53,741
Last modified:February 1, 1995 - v1
Checksum:i131792A392CACCC0
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 81W → L AA sequence 1 Publication
Sequence conflicti12 – 121E → G AA sequence 1 Publication
Sequence conflicti17 – 171R → A AA sequence 1 Publication
Sequence conflicti19 – 191E → G AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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: July 9, 2014
This is version 70 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

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