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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)DescriptionActionsGraphical viewLength
Binding sitei172L-threo-beta-methylaspartate1 Publication1
Sitei194Transition state stabilizer1
Metal bindingi238Magnesium1 Publication1
Metal bindingi273Magnesium1 Publication1
Metal bindingi307Magnesium1 Publication1
Binding sitei329L-threo-beta-methylaspartate1 Publication1
Active sitei331Proton acceptor1 Publication1

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeCitrobacter

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004293671 – 413Methylaspartate ammonia-lyaseAdd BLAST413

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1413
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 18Combined sources17
Helixi20 – 24Combined sources5
Beta strandi44 – 59Combined sources16
Beta strandi64 – 69Combined sources6
Turni73 – 76Combined sources4
Helixi86 – 96Combined sources11
Helixi98 – 101Combined sources4
Helixi110 – 118Combined sources9
Helixi128 – 145Combined sources18
Helixi150 – 157Combined sources8
Helixi179 – 186Combined sources8
Beta strandi190 – 194Combined sources5
Helixi200 – 204Combined sources5
Helixi209 – 225Combined sources17
Beta strandi234 – 238Combined sources5
Helixi242 – 246Combined sources5
Turni247 – 249Combined sources3
Helixi251 – 260Combined sources10
Helixi261 – 265Combined sources5
Beta strandi270 – 273Combined sources4
Helixi281 – 298Combined sources18
Beta strandi303 – 306Combined sources4
Helixi313 – 321Combined sources9
Beta strandi326 – 330Combined sources5
Helixi332 – 335Combined sources4
Helixi339 – 351Combined sources13
Beta strandi354 – 357Combined sources4
Helixi365 – 378Combined sources14
Beta strandi381 – 384Combined sources4
Beta strandi389 – 391Combined sources3
Helixi392 – 410Combined sources19

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiO66145.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni360 – 361L-threo-beta-methylaspartate binding2

Sequence similaritiesi

Family and domain databases

CDDicd03314. MAL. 1 hit.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KKOX-ray1.33A/B1-413[»]
1KKRX-ray2.10A/B1-413[»]
ProteinModelPortaliO66145.
SMRiO66145.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00561; UER00618.

Miscellaneous databases

EvolutionaryTraceiO66145.

Family and domain databases

CDDicd03314. MAL. 1 hit.
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 2, 2016
This is version 50 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.