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Protein

Methylaspartate ammonia-lyase

Gene
N/A
Organism
Citrobacter amalonaticus
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the methylaspartate cycle. Catalyzes the formation of the alpha,beta-unsaturated bond by the reversible anti elimination of ammonia from L-threo-beta-methylaspartate (L-threo-(2S,3S)-3-methylaspartate) to give mesaconate (By similarity).By similarity

Catalytic activityi

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

Cofactori

Mg2+1 Publication

Pathwayi: L-glutamate degradation via mesaconate pathway

This protein is involved in step 2 of the subpathway that synthesizes acetate and pyruvate from L-glutamate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Glutamate mutase epsilon subunit (glmE), Glutamate mutase sigma subunit (glmS), Glutamate mutase epsilon subunit (glmE), Glutamate mutase sigma subunit (glmS), Glutamate mutase epsilon subunit (glmE)
  2. Methylaspartate ammonia-lyase
  3. no protein annotated in this organism
  4. no protein annotated in this organism
This subpathway is part of the pathway L-glutamate degradation via mesaconate pathway, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes acetate and pyruvate from L-glutamate, the pathway L-glutamate degradation via mesaconate pathway and in Amino-acid degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei172 – 1721L-threo-beta-methylaspartate1 Publication
Sitei194 – 1941Transition state stabilizer
Metal bindingi238 – 2381Magnesium1 Publication
Metal bindingi273 – 2731Magnesium1 Publication
Metal bindingi307 – 3071Magnesium1 Publication
Binding sitei329 – 3291L-threo-beta-methylaspartate1 Publication
Active sitei331 – 3311Proton acceptor1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00561; UER00618.

Names & Taxonomyi

Protein namesi
Recommended name:
Methylaspartate ammonia-lyase (EC:4.3.1.2)
Short name:
MAL
Alternative name(s):
3-methylaspartate ammonia-lyase
Beta-methylaspartase
OrganismiCitrobacter amalonaticus
Taxonomic identifieri35703 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeCitrobacter

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 413413Methylaspartate ammonia-lyasePRO_0000429367Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1
413
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 1817Combined sources
Helixi20 – 245Combined sources
Beta strandi44 – 5916Combined sources
Beta strandi64 – 696Combined sources
Turni73 – 764Combined sources
Helixi86 – 9611Combined sources
Helixi98 – 1014Combined sources
Helixi110 – 1189Combined sources
Helixi128 – 14518Combined sources
Helixi150 – 1578Combined sources
Helixi179 – 1868Combined sources
Beta strandi190 – 1945Combined sources
Helixi200 – 2045Combined sources
Helixi209 – 22517Combined sources
Beta strandi234 – 2385Combined sources
Helixi242 – 2465Combined sources
Turni247 – 2493Combined sources
Helixi251 – 26010Combined sources
Helixi261 – 2655Combined sources
Beta strandi270 – 2734Combined sources
Helixi281 – 29818Combined sources
Beta strandi303 – 3064Combined sources
Helixi313 – 3219Combined sources
Beta strandi326 – 3305Combined sources
Helixi332 – 3354Combined sources
Helixi339 – 35113Combined sources
Beta strandi354 – 3574Combined sources
Helixi365 – 37814Combined sources
Beta strandi381 – 3844Combined sources
Beta strandi389 – 3913Combined sources
Helixi392 – 41019Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KKOX-ray1.33A/B1-413[»]
1KKRX-ray2.10A/B1-413[»]
ProteinModelPortaliO66145.
SMRiO66145. Positions 1-411.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO66145.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni360 – 3612L-threo-beta-methylaspartate binding

Sequence similaritiesi

Family and domain databases

Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
InterProiIPR029065. Enolase_C-like.
IPR029017. Enolase_N-like.
IPR006395. Me_Asp_am_lyase.
IPR022662. MeAsp_NH4-lyase_C.
IPR022665. MeAsp_NH4-lyase_N.
IPR001354. MR/MLE/MAL.
[Graphical view]
PANTHERiPTHR13794. PTHR13794. 2 hits.
PfamiPF07476. MAAL_C. 1 hit.
PF05034. MAAL_N. 1 hit.
[Graphical view]
PIRSFiPIRSF017107. MAL. 1 hit.
SUPFAMiSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsiTIGR01502. B_methylAsp_ase. 1 hit.

Sequencei

Sequence statusi: Complete.

O66145-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKIKQALFTA GYSSFYFDDQ QAIKNGAGHD GFIYTGDPVT PGFTSVRQAG
60 70 80 90 100
ECVSVQLILE NGAVAVGDCA AVQYSGAGGR DPLFLAEHFI PFLNDHIKPL
110 120 130 140 150
LEGRDVDAFL PNARFFDKLR IDGNLLHTAV RYGLSQALLD ATALASGRLK
160 170 180 190 200
TEVVCDEWQL PCVPEAIPLF GQSGDDRYIA VDKMILKGVD VLPHALINNV
210 220 230 240 250
EEKLGFKGEK LREYVRWLSD RILSLRSSPR YHPTLHIDVY GTIGLIFDMD
260 270 280 290 300
PVRCAEYIAS LEKEAQGLPL YIEGPVDAGN KPDQIRMLTA ITKELTRLGS
310 320 330 340 350
GVKIVADEWC NTYQDIVDFT DAGSCHMVQI KTPDLGGIHN IVDAVLYCNK
360 370 380 390 400
HGMEAYQGGT CNETEISART CVHVALAARP MRMLIKPGMG FDEGLNIVFN
410
EMNRTIALLQ TKD
Length:413
Mass (Da):45,471
Last modified:August 1, 1998 - v1
Checksum:iE6101562FDD6DD99
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB005294 Genomic DNA. Translation: BAA28709.1.
PIRiT43810.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB005294 Genomic DNA. Translation: BAA28709.1.
PIRiT43810.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KKOX-ray1.33A/B1-413[»]
1KKRX-ray2.10A/B1-413[»]
ProteinModelPortaliO66145.
SMRiO66145. Positions 1-411.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00561; UER00618.

Miscellaneous databases

EvolutionaryTraceiO66145.

Family and domain databases

Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
InterProiIPR029065. Enolase_C-like.
IPR029017. Enolase_N-like.
IPR006395. Me_Asp_am_lyase.
IPR022662. MeAsp_NH4-lyase_C.
IPR022665. MeAsp_NH4-lyase_N.
IPR001354. MR/MLE/MAL.
[Graphical view]
PANTHERiPTHR13794. PTHR13794. 2 hits.
PfamiPF07476. MAAL_C. 1 hit.
PF05034. MAAL_N. 1 hit.
[Graphical view]
PIRSFiPIRSF017107. MAL. 1 hit.
SUPFAMiSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsiTIGR01502. B_methylAsp_ase. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiMAAL_CITAM
AccessioniPrimary (citable) accession number: O66145
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 11, 2014
Last sequence update: August 1, 1998
Last modified: November 11, 2015
This is version 48 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

3D-structure

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.