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Q05514 (MAAL_CLOTT) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methylaspartate ammonia-lyase

EC=4.3.1.2
Alternative name(s):
Beta-methylaspartase
OrganismClostridium tetanomorphum
Taxonomic identifier1553 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length413 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

L-threo-3-methylaspartate = mesaconate + NH3.

Pathway

Amino-acid degradation; L-glutamate degradation via mesaconate pathway; acetate and pyruvate from L-glutamate: step 2/4.

Subunit structure

Homodimer.

Ontologies

Keywords
   LigandCobalamin
Cobalt
   Molecular functionLyase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processglutamate catabolic process via L-citramalate

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functioncobalamin binding

Inferred from electronic annotation. Source: UniProtKB-KW

methylaspartate ammonia-lyase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 413413Methylaspartate ammonia-lyase
PRO_0000084547

Secondary structure

................................................................... 413
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q05514 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 4451923DB035EF13

FASTA41345,534
        10         20         30         40         50         60 
MKIVDVLCTP GLTGFYFDDQ RAIKKGAGHD GFTYTGSTVT EGFTQVRQKG ESISVLLVLE 

        70         80         90        100        110        120 
DGQVAHGDCA AVQYSGAGGR DPLFLAKDFI PVIEKEIAPK LIGREITNFK PMAEEFDKMT 

       130        140        150        160        170        180 
VNGNRLHTAI RYGITQAILD AVAKTRKVTM AEVIRDEYNP GAEINAVPVF AQSGDDRYDN 

       190        200        210        220        230        240 
VDKMIIKEAD VLPHALINNV EEKLGLKGEK LLEYVKWLRD RIIKLRVRED YAPIFHIDVY 

       250        260        270        280        290        300 
GTIGAAFDVD IKAMADYIQT LAEAAKPFHL RIEGPMDVED RQKQMEAMRD LRAELDGRGV 

       310        320        330        340        350        360 
DAELVADEWC NTVEDVKFFT DNKAGHMVQI KTPDLGGVNN IADAIMYCKA NGMGAYCGGT 

       370        380        390        400        410 
CNETNRSAEV TTNIGMACGA RQVLAKPGMG VDEGMMIVKN EMNRVLALVG RRK 

« Hide

References

[1]"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], PROTEIN SEQUENCE OF 1-26.
Strain: ATCC 15920 / DSM 528 / H1.
[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] OF 1-24, PROTEIN SEQUENCE OF 1-24.
Strain: ATCC 15920 / DSM 528 / H1.
[3]"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] OF 1-71.
Strain: NCIMB 11547.
[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 1-15.
Strain: NCIMB 11547.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S48141 Genomic DNA. Translation: AAB24070.1.
X70499 Genomic DNA. Translation: CAA49911.1.
X70695 Genomic DNA. Translation: CAA50027.1.
PIRB44285.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KCZX-ray1.90A/B1-413[»]
1KD0X-ray1.90A/B1-413[»]
3ZVHX-ray1.99A/B1-413[»]
3ZVIX-ray1.90A/B1-413[»]
ProteinModelPortalQ05514.
SMRQ05514. Positions 1-413.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-1103.
UniPathwayUPA00561; UER00618.

Family and domain databases

InterProIPR006395. Me_Asp_am_lyase.
IPR022662. MeAsp_NH4-lyase_C.
IPR022665. MeAsp_NH4-lyase_N.
IPR001354. MR_MLE.
[Graphical view]
PANTHERPTHR13794. PTHR13794. 1 hit.
PfamPF07476. MAAL_C. 1 hit.
PF05034. MAAL_N. 1 hit.
[Graphical view]
PIRSFPIRSF017107. MAL. 1 hit.
TIGRFAMsTIGR01502. B_methylAsp_ase. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ05514.

Entry information

Entry nameMAAL_CLOTT
AccessionPrimary (citable) accession number: Q05514
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: October 16, 2013
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways