UniProtKB - Q05514 (MAAL_CLOTT)
Protein
Methylaspartate ammonia-lyase
Gene
N/A
Organism
Clostridium tetanomorphum
Status
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. It can also use L-erythro-beta-methylaspartate (L-erythro-(2S,3R)-3-methylaspartate), L-aspartate, fumarate and ethylfumarate as substrates.4 Publications
Catalytic activityi
- EC:4.3.1.24 Publications
Cofactori
Mg2+3 Publications
Activity regulationi
Inhibited by calcium ions.1 Publication
Kineticsi
Kcat is 61 sec(-1) for amination of mesaconate (with 20 mM of MgCl2 at pH 9 and at 30 degrees Celsius). Kcat is 89 sec(-1) for deamination of L-threo-beta-methylaspartate (with 20 mM of MgCl2 at pH 9 and at 30 degrees Celsius).
- KM=0.65 mM for L-threo-beta-methylaspartate (with 4 mM of KCl at pH 9.76 and at 25 degrees Celsius)3 Publications
- KM=0.67 mM for L-threo-beta-methylaspartate (with 50 mM of KCl at pH 9 and at 30 degrees Celsius)3 Publications
- KM=0.7 mM for mesaconate (with 20 mM of MgCl2 at pH 9 and at 30 degrees Celsius)3 Publications
- KM=1 mM for L-threo-beta-methylaspartate (with 20 mM of MgCl2 at pH 9 and at 30 degrees Celsius)3 Publications
- KM=2.3 mM for L-aspartate (with 4 mM of KCl at pH 9.76 and at 25 degrees Celsius)3 Publications
- KM=2.8 mM for L-threo-beta-methylaspartate (with 0.3 mM of KCl at pH 9 and at 30 degrees Celsius)3 Publications
- Vmax=2089 µmol/min/mg enzyme with L-threo-beta-methylaspartate as substrate (with 50 mM of KCl at pH 9 and at 30 degrees Celsius)3 Publications
- Vmax=309 µmol/min/mg enzyme with L-threo-beta-methylaspartate as substrate (with 0.3 mM of KCl at pH 9 and at 30 degrees Celsius)3 Publications
- Vmax=266 µmol/min/mg enzyme with L-threo-beta-methylaspartate as substrate (with 4 mM of KCl at pH 9.76 and at 25 degrees Celsius)3 Publications
- Vmax=2.5 µmol/min/mg enzyme with L-erythro-beta-methylaspartate as substrate (with 4 mM of KCl at pH 9.76 and at 25 degrees Celsius)3 Publications
- Vmax=2.4 µmol/min/mg enzyme with L-aspartate as substrate (with 4 mM of KCl at pH 9.76 and at 25 degrees Celsius)3 Publications
pH dependencei
Optimum pH is 9.7.3 Publications
Temperature dependencei
Optimum temperature is 55 degrees Celsius. It retains only half of its original activity after a 30 minutes incubation period at 50 degrees Celsius.3 Publications
: L-glutamate degradation via mesaconate pathway Pathwayi
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:
- Glutamate mutase epsilon subunit (glmE), Glutamate mutase sigma subunit (glmS)
- Methylaspartate ammonia-lyase
- no protein annotated in this organism
- no protein annotated in this organism
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 172 | L-threo-beta-methylaspartateBy similarity | 1 | |
Sitei | 194 | Transition state stabilizer | 1 | |
Metal bindingi | 238 | Magnesium2 Publications | 1 | |
Metal bindingi | 273 | Magnesium2 Publications | 1 | |
Metal bindingi | 307 | Magnesium2 Publications | 1 | |
Binding sitei | 329 | L-threo-beta-methylaspartate | 1 | |
Active sitei | 331 | Proton acceptor2 Publications | 1 | |
Binding sitei | 361 | L-threo-beta-methylaspartate | 1 |
GO - Molecular functioni
- cobalamin binding Source: UniProtKB-KW
- metal ion binding Source: UniProtKB-KW
- methylaspartate ammonia-lyase activity Source: UniProtKB-EC
GO - Biological processi
- glutamate catabolic process via L-citramalate Source: UniProtKB-UniPathway
Keywordsi
Molecular function | Lyase |
Ligand | Cobalamin, Cobalt, Magnesium, Metal-binding |
Enzyme and pathway databases
BioCyci | MetaCyc:MONOMER-1103 |
BRENDAi | 4.3.1.2, 1527 |
UniPathwayi | UPA00561;UER00618 |
Names & Taxonomyi
Protein namesi | Recommended name: Methylaspartate ammonia-lyase (EC:4.3.1.2)Short name: MAL Alternative name(s): 3-methylaspartase ammonia-lyase Beta-methylaspartase |
Organismi | Clostridium tetanomorphum |
Taxonomic identifieri | 1553 [NCBI] |
Taxonomic lineagei | Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium |
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 73 | Q → A: It has very broad nucleophile scope and excellent regio- and diastereoselectivity in the amination reaction. This mutation strongly moves the specificity of MAL away from ammonia and towards methylamine. It is highly enantioselective. 1 Publication | 1 | |
Mutagenesisi | 194 | H → A: Strong (160-fold) decrease of the catalytic efficiency for deamination and slight (1.8-fold) decrease of affinity binding for L-threo-beta-methylaspartate. 7-fold decrease of the catalytic efficiency for amination and 20-fold decrease of affinity binding for mesaconate. It does not show any major conformational changes. 1 Publication | 1 | |
Mutagenesisi | 194 | H → R: It abolishes deaminase and aminase activities and does not show any major conformational changes. 1 Publication | 1 | |
Mutagenesisi | 329 | Q → A: Very strong decrease of the catalytic efficiency for deamination, whereas the affinity binding for L-threo-beta-methylaspartate is not affected. Strong (240-fold) decrease of the catalytic efficiency for amination and slight (2.4-fold) decrease of affinity binding for mesaconate. It does not show any major conformational changes. 1 Publication | 1 | |
Mutagenesisi | 329 | Q → R: It abolishes deaminase and aminase activities and does not show any major conformational changes. 1 Publication | 1 | |
Mutagenesisi | 331 | K → A: It abolishes deaminase and aminase activities and does not show any major conformational changes. 1 Publication | 1 | |
Mutagenesisi | 331 | K → G: It abolishes deaminase and aminase activities and does not show any major conformational changes. 1 Publication | 1 | |
Mutagenesisi | 331 | K → H: It abolishes deaminase and aminase activities and does not show any major conformational changes. 1 Publication | 1 | |
Mutagenesisi | 331 | K → Q: It abolishes deaminase and aminase activities and does not show any major conformational changes. 1 Publication | 1 | |
Mutagenesisi | 331 | K → R: It abolishes deaminase and aminase activities and does not show any major conformational changes. 1 Publication | 1 | |
Mutagenesisi | 384 | L → A: It has very broad electrophile scope and excellent regio- and enantioselectivity in the amination reaction. 1 Publication | 1 |
Chemistry databases
DrugBanki | DB03661, L-cysteic acid |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000084547 | 1 – 413 | Methylaspartate ammonia-lyaseAdd BLAST | 413 |
Interactioni
Subunit structurei
Homodimer.
4 PublicationsStructurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | Q05514 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q05514 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 360 – 361 | L-threo-beta-methylaspartate bindingBy similarity | 2 |
Sequence similaritiesi
Belongs to the methylaspartate ammonia-lyase family.Curated
Family and domain databases
CDDi | cd03314, MAL, 1 hit |
Gene3Di | 3.20.20.120, 1 hit 3.30.390.10, 1 hit |
InterProi | View protein in InterPro IPR036849, Enolase-like_C_sf IPR029017, Enolase-like_N IPR006395, Me_Asp_am_lyase IPR022662, MeAsp_NH4-lyase_C IPR022665, MeAsp_NH4-lyase_N |
Pfami | View protein in Pfam PF07476, MAAL_C, 1 hit PF05034, MAAL_N, 1 hit |
PIRSFi | PIRSF017107, MAL, 1 hit |
SFLDi | SFLDG00151, methylaspartate_ammonia-lyase, 1 hit |
SUPFAMi | SSF51604, SSF51604, 1 hit SSF54826, SSF54826, 1 hit |
TIGRFAMsi | TIGR01502, B_methylAsp_ase, 1 hit |
i Sequence
Sequence statusi: Complete.
Q05514-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MKIVDVLCTP GLTGFYFDDQ RAIKKGAGHD GFTYTGSTVT EGFTQVRQKG
60 70 80 90 100
ESISVLLVLE DGQVAHGDCA AVQYSGAGGR DPLFLAKDFI PVIEKEIAPK
110 120 130 140 150
LIGREITNFK PMAEEFDKMT VNGNRLHTAI RYGITQAILD AVAKTRKVTM
160 170 180 190 200
AEVIRDEYNP GAEINAVPVF AQSGDDRYDN VDKMIIKEAD VLPHALINNV
210 220 230 240 250
EEKLGLKGEK LLEYVKWLRD RIIKLRVRED YAPIFHIDVY GTIGAAFDVD
260 270 280 290 300
IKAMADYIQT LAEAAKPFHL RIEGPMDVED RQKQMEAMRD LRAELDGRGV
310 320 330 340 350
DAELVADEWC NTVEDVKFFT DNKAGHMVQI KTPDLGGVNN IADAIMYCKA
360 370 380 390 400
NGMGAYCGGT CNETNRSAEV TTNIGMACGA RQVLAKPGMG VDEGMMIVKN
410
EMNRVLALVG RRK
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | S48141 Genomic DNA Translation: AAB24070.1 X70499 Genomic DNA Translation: CAA49911.1 X70695 Genomic DNA Translation: CAA50027.1 |
PIRi | B44285 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | S48141 Genomic DNA Translation: AAB24070.1 X70499 Genomic DNA Translation: CAA49911.1 X70695 Genomic DNA Translation: CAA50027.1 |
PIRi | B44285 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1KCZ | X-ray | 1.90 | A/B | 1-413 | [»] | |
1KD0 | X-ray | 1.90 | A/B | 1-413 | [»] | |
3ZVH | X-ray | 1.99 | A/B | 1-413 | [»] | |
3ZVI | X-ray | 1.90 | A/B | 1-413 | [»] | |
SMRi | Q05514 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Chemistry databases
DrugBanki | DB03661, L-cysteic acid |
Enzyme and pathway databases
UniPathwayi | UPA00561;UER00618 |
BioCyci | MetaCyc:MONOMER-1103 |
BRENDAi | 4.3.1.2, 1527 |
Miscellaneous databases
EvolutionaryTracei | Q05514 |
Family and domain databases
CDDi | cd03314, MAL, 1 hit |
Gene3Di | 3.20.20.120, 1 hit 3.30.390.10, 1 hit |
InterProi | View protein in InterPro IPR036849, Enolase-like_C_sf IPR029017, Enolase-like_N IPR006395, Me_Asp_am_lyase IPR022662, MeAsp_NH4-lyase_C IPR022665, MeAsp_NH4-lyase_N |
Pfami | View protein in Pfam PF07476, MAAL_C, 1 hit PF05034, MAAL_N, 1 hit |
PIRSFi | PIRSF017107, MAL, 1 hit |
SFLDi | SFLDG00151, methylaspartate_ammonia-lyase, 1 hit |
SUPFAMi | SSF51604, SSF51604, 1 hit SSF54826, SSF54826, 1 hit |
TIGRFAMsi | TIGR01502, B_methylAsp_ase, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | MAAL_CLOTT | |
Accessioni | Q05514Primary (citable) accession number: Q05514 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | February 1, 1995 |
Last sequence update: | February 1, 1995 | |
Last modified: | December 2, 2020 | |
This is version 100 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencingDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families