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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 PublicationsUniRule annotation

Catalytic activityi

L-threo-3-methylaspartate = L-glutamate.2 PublicationsUniRule annotation

Cofactori

adenosylcob(III)alamin4 PublicationsUniRule annotation

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

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 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
OrganismiClostridium cochlearium
Taxonomic identifieri1494 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 483483Glutamate mutase epsilon subunitPRO_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 PublicationsUniRule annotation

Binary interactionsi

WithEntry#Exp.IntActNotes
glmSP800782EBI-1028142,EBI-1028147

Protein-protein interaction databases

IntActiP80077. 1 interaction.

Structurei

Secondary structure

1
483
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 2011Combined sources
Helixi21 – 233Combined sources
Helixi25 – 295Combined sources
Helixi32 – 409Combined sources
Helixi44 – 463Combined sources
Helixi48 – 5811Combined sources
Beta strandi62 – 643Combined sources
Helixi72 – 8413Combined sources
Beta strandi89 – 957Combined sources
Helixi99 – 1013Combined sources
Helixi104 – 11714Combined sources
Beta strandi122 – 1254Combined sources
Helixi127 – 14115Combined sources
Beta strandi146 – 1494Combined sources
Helixi156 – 1649Combined sources
Beta strandi169 – 1713Combined sources
Turni174 – 1818Combined sources
Helixi187 – 20620Combined sources
Beta strandi212 – 2143Combined sources
Turni217 – 2204Combined sources
Beta strandi221 – 2233Combined sources
Helixi226 – 24217Combined sources
Beta strandi247 – 2537Combined sources
Helixi258 – 27821Combined sources
Beta strandi285 – 2917Combined sources
Helixi301 – 31818Combined sources
Beta strandi321 – 3244Combined sources
Turni328 – 3325Combined sources
Helixi337 – 35317Combined sources
Turni354 – 3563Combined sources
Helixi363 – 38624Combined sources
Turni387 – 3893Combined sources
Helixi391 – 40010Combined sources
Beta strandi419 – 4224Combined sources
Beta strandi428 – 4325Combined sources
Helixi440 – 45718Combined sources
Helixi463 – 47210Combined sources
Turni473 – 4764Combined sources
Beta strandi477 – 4793Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80077.

Family & Domainsi

Region

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

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.

P80077-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MELKNKKWTD EEFHKQREEV LQQWPTGKEV DLQEAVDYLK KIPAEKNFAE
60 70 80 90 100
KLVLAKKKGI TMAQPRAGVA LLDEHIELLR YLQDEGGADF LPSTIDAYTR
110 120 130 140 150
QNRYDECENG IKESEKAGRS LLNGFPGVNY GVKGCRKVLE AVNLPLQARH
160 170 180 190 200
GTPDSRLLAE IIHAGGWTSN EGGGISYNVP YAKNVTIEKS LLDWQYCDRL
210 220 230 240 250
VGFYEEQGVH INREPFGPLT GTLVPPSMSN AVGITEALLA AEQGVKNITV
260 270 280 290 300
GYGECGNMIQ DIAALRCLEE QTNEYLKAYG YNDVFVTTVF HQWMGGFPQD
310 320 330 340 350
ESKAFGVIVT ATTIAALAGA TKVIVKTPHE AIGIPTKEAN AAGIKATKMA
360 370 380 390 400
LNMLEGQRMP MSKELETEMA VIKAETKCIL DKMFELGKGD LAIGTVKAFE
410 420 430 440 450
TGVMDIPFGP SKYNAGKMMP VRDNLGCVRY LEFGNVPFTE EIKNYNRERL
460 470 480
QERAKFEGRD VSFQMVIDDI FAVGKGRLIG RPE
Length:483
Mass (Da):53,574
Last modified:November 1, 1997 - v2
Checksum:i0789965B945B3F5C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X80997 Genomic DNA. Translation: CAA56923.1.
PIRiI40662.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X80997 Genomic DNA. Translation: CAA56923.1 .
PIRi I40662.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 87 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