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P80077

- GLME_CLOCO

UniProt

P80077 - GLME_CLOCO

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Protein
Glutamate mutase epsilon subunit
Gene
glmE
Organism
Clostridium cochlearium
Status
Reviewed - Annotation score: 5 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).2 Publications

Catalytic activityi

L-threo-3-methylaspartate = L-glutamate.2 Publications

Cofactori

Adenosylcobalamin.4 Publications

Enzyme regulationi

Competitively inhibited by (2S,4S)-4-fluoroglutamate, 2-methyleneglutarate, (2R,3RS)-3-fluoroglutamate and (S)-3-methylitaconate.2 Publications

Pathwayi

Sites

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

GO - Molecular functioni

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

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

BioCyciMetaCyc:MONOMER-1101.
SABIO-RKP80077.
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
OrganismiClostridium cochlearium
Taxonomic identifieri1494 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 483483Glutamate mutase epsilon subunitUniRule annotation
PRO_0000087511Add
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.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
mamAP800782EBI-1028142,EBI-1028147

Protein-protein interaction databases

IntActiP80077. 1 interaction.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 2011
Helixi21 – 233
Helixi25 – 295
Helixi32 – 409
Helixi44 – 463
Helixi48 – 5811
Beta strandi62 – 643
Helixi72 – 8413
Beta strandi89 – 957
Helixi99 – 1013
Helixi104 – 11714
Beta strandi122 – 1254
Helixi127 – 14115
Beta strandi146 – 1494
Helixi156 – 1649
Beta strandi169 – 1713
Turni174 – 1818
Helixi187 – 20620
Beta strandi212 – 2143
Turni217 – 2204
Beta strandi221 – 2233
Helixi226 – 24217
Beta strandi247 – 2537
Helixi258 – 27821
Beta strandi285 – 2917
Helixi301 – 31818
Beta strandi321 – 3244
Turni328 – 3325
Helixi337 – 35317
Turni354 – 3563
Helixi363 – 38624
Turni387 – 3893
Helixi391 – 40010
Beta strandi419 – 4224
Beta strandi428 – 4325
Helixi440 – 45718
Helixi463 – 47210
Turni473 – 4764
Beta strandi477 – 4793

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CB7X-ray2.00B/D1-483[»]
1CCWX-ray1.60B/D1-483[»]
1I9CX-ray1.90B/D1-483[»]
ProteinModelPortaliP80077.
SMRiP80077. Positions 1-483.

Miscellaneous databases

EvolutionaryTraceiP80077.

Family & Domainsi

Region

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

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.

P80077-1 [UniParc]FASTAAdd to Basket

« Hide

MELKNKKWTD EEFHKQREEV LQQWPTGKEV DLQEAVDYLK KIPAEKNFAE    50
KLVLAKKKGI TMAQPRAGVA LLDEHIELLR YLQDEGGADF LPSTIDAYTR 100
QNRYDECENG IKESEKAGRS LLNGFPGVNY GVKGCRKVLE AVNLPLQARH 150
GTPDSRLLAE IIHAGGWTSN EGGGISYNVP YAKNVTIEKS LLDWQYCDRL 200
VGFYEEQGVH INREPFGPLT GTLVPPSMSN AVGITEALLA AEQGVKNITV 250
GYGECGNMIQ DIAALRCLEE QTNEYLKAYG YNDVFVTTVF HQWMGGFPQD 300
ESKAFGVIVT ATTIAALAGA TKVIVKTPHE AIGIPTKEAN AAGIKATKMA 350
LNMLEGQRMP MSKELETEMA VIKAETKCIL DKMFELGKGD LAIGTVKAFE 400
TGVMDIPFGP SKYNAGKMMP VRDNLGCVRY LEFGNVPFTE EIKNYNRERL 450
QERAKFEGRD VSFQMVIDDI FAVGKGRLIG RPE 483
Length:483
Mass (Da):53,574
Last modified:November 1, 1997 - v2
Checksum:i0789965B945B3F5C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X80997 Genomic DNA. Translation: CAA56923.1.
PIRiI40662.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X80997 Genomic DNA. Translation: CAA56923.1 .
PIRi I40662.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CB7 X-ray 2.00 B/D 1-483 [» ]
1CCW X-ray 1.60 B/D 1-483 [» ]
1I9C X-ray 1.90 B/D 1-483 [» ]
ProteinModelPortali P80077.
SMRi P80077. Positions 1-483.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P80077. 1 interaction.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00561 ; UER00617 .
BioCyci MetaCyc:MONOMER-1101.
SABIO-RK P80077.

Miscellaneous databases

EvolutionaryTracei P80077.

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. "Characterization of the coenzyme-B12-dependent glutamate mutase from Clostridium cochlearium produced in Escherichia coli."
    Zelder O., Beatrix B., Leutbecher U., Buckel W.
    Eur. J. Biochem. 226:577-585(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, COFACTOR, SUBUNIT.
    Strain: ATCC 17787 / DSM 1285 / NCIB 10633.
  2. "Glutamate mutase from Clostridium cochlearium. Purification, cobamide content and stereospecific inhibitors."
    Leutbecher U., Boecher R., Linder D., Buckel W.
    Eur. J. Biochem. 205:759-765(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-26, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, COFACTOR, SUBUNIT.
    Strain: ATCC 17787 / DSM 1285 / NCIB 10633.
  3. "Glutamate mutase from Clostridium cochlearium: the structure of a coenzyme B12-dependent enzyme provides new mechanistic insights."
    Reitzer R., Gruber K., Jogl G., Wagner U.G., Bothe H., Buckel W., Kratky C.
    Structure 7:891-902(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH COBALAMIN ANALOGS, COFACTOR, SUBUNIT.
    Strain: ATCC 17787 / DSM 1285 / NCIB 10633.
  4. "Radical shuttling in a protein: ribose pseudorotation controls alkyl-radical transfer in the coenzyme B(12) dependent enzyme glutamate mutase."
    Gruber K., Reitzer R., Kratky C.
    Angew. Chem. Int. Ed. Engl. 40:3377-3380(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH COBALAMIN ANALOGS AND SUBSTRATE, COFACTOR, SUBUNIT.

Entry informationi

Entry nameiGLME_CLOCO
AccessioniPrimary (citable) accession number: P80077
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: November 1, 1997
Last modified: July 9, 2014
This is version 84 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

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

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