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Methylaspartate ammonia-lyase (MAL) (EC 4.3.1.2) (3-methylaspartate ammonia-lyase) (Beta-methylaspartase)

 MAAL_CITAM              Reviewed;         413 AA.
O66145;
11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 1.
28-FEB-2018, entry version 57.
RecName: Full=Methylaspartate ammonia-lyase;
Short=MAL;
EC=4.3.1.2;
AltName: Full=3-methylaspartate ammonia-lyase;
AltName: Full=Beta-methylaspartase;
Citrobacter amalonaticus.
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Citrobacter.
NCBI_TaxID=35703;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=YG-1002;
PubMed=9830098; DOI=10.1007/s002530051322;
Kato Y., Asano Y.;
"Cloning, nucleotide sequencing, and expression of the 3-
methylaspartate ammonia-lyase gene from Citrobacter amalonaticus
strain YG-1002.";
Appl. Microbiol. Biotechnol. 50:468-474(1998).
[2]
X-RAY CRYSTALLOGRAPHY (1.33 ANGSTROMS) IN COMPLEX WITH
L-THREO-BETA-METHYLASPARTATE AND MAGNESIUM, ACTIVE SITE, COFACTOR, AND
SUBUNIT.
PubMed=11796115; DOI=10.1016/S0969-2126(01)00696-7;
Levy C.W., Buckley P.A., Sedelnikova S., Kato Y., Asano Y., Rice D.W.,
Baker P.J.;
"Insights into enzyme evolution revealed by the structure of
methylaspartate ammonia lyase.";
Structure 10:105-113(2002).
-!- FUNCTION: 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). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: L-threo-3-methylaspartate = mesaconate +
NH(3).
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:11796115};
-!- PATHWAY: Amino-acid degradation; L-glutamate degradation via
mesaconate pathway; acetate and pyruvate from L-glutamate: step
2/4.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11796115}.
-!- SIMILARITY: Belongs to the methylaspartate ammonia-lyase family.
{ECO:0000305}.
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EMBL; AB005294; BAA28709.1; -; Genomic_DNA.
PIR; T43810; T43810.
PDB; 1KKO; X-ray; 1.33 A; A/B=1-413.
PDB; 1KKR; X-ray; 2.10 A; A/B=1-413.
PDBsum; 1KKO; -.
PDBsum; 1KKR; -.
ProteinModelPortal; O66145; -.
SMR; O66145; -.
UniPathway; UPA00561; UER00618.
EvolutionaryTrace; O66145; -.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0050096; F:methylaspartate ammonia-lyase activity; IEA:UniProtKB-EC.
GO; GO:0019553; P:glutamate catabolic process via L-citramalate; IEA:UniProtKB-UniPathway.
CDD; cd03314; MAL; 1.
Gene3D; 3.20.20.120; -; 1.
Gene3D; 3.30.390.10; -; 1.
InterPro; IPR036849; Enolase-like_C_sf.
InterPro; IPR029017; Enolase-like_N.
InterPro; IPR034390; Enolase-like_superfamily.
InterPro; IPR006395; Me_Asp_am_lyase.
InterPro; IPR022662; MeAsp_NH4-lyase_C.
InterPro; IPR022665; MeAsp_NH4-lyase_N.
Pfam; PF07476; MAAL_C; 1.
Pfam; PF05034; MAAL_N; 1.
PIRSF; PIRSF017107; MAL; 1.
SFLD; SFLDG00151; methylaspartate_ammonia-lyase; 1.
SFLD; SFLDS00001; Enolase; 1.
SUPFAM; SSF51604; SSF51604; 1.
TIGRFAMs; TIGR01502; B_methylAsp_ase; 1.
1: Evidence at protein level;
3D-structure; Lyase; Magnesium; Metal-binding.
CHAIN 1 413 Methylaspartate ammonia-lyase.
/FTId=PRO_0000429367.
REGION 360 361 L-threo-beta-methylaspartate binding.
ACT_SITE 331 331 Proton acceptor.
{ECO:0000269|PubMed:11796115}.
METAL 238 238 Magnesium. {ECO:0000269|PubMed:11796115}.
METAL 273 273 Magnesium. {ECO:0000269|PubMed:11796115}.
METAL 307 307 Magnesium. {ECO:0000269|PubMed:11796115}.
BINDING 172 172 L-threo-beta-methylaspartate.
{ECO:0000269|PubMed:11796115}.
BINDING 329 329 L-threo-beta-methylaspartate.
{ECO:0000269|PubMed:11796115}.
SITE 194 194 Transition state stabilizer.
STRAND 2 18 {ECO:0000244|PDB:1KKO}.
HELIX 20 24 {ECO:0000244|PDB:1KKO}.
STRAND 44 59 {ECO:0000244|PDB:1KKO}.
STRAND 64 69 {ECO:0000244|PDB:1KKO}.
TURN 73 76 {ECO:0000244|PDB:1KKO}.
HELIX 86 96 {ECO:0000244|PDB:1KKO}.
HELIX 98 101 {ECO:0000244|PDB:1KKO}.
HELIX 110 118 {ECO:0000244|PDB:1KKO}.
HELIX 128 145 {ECO:0000244|PDB:1KKO}.
HELIX 150 157 {ECO:0000244|PDB:1KKO}.
HELIX 179 186 {ECO:0000244|PDB:1KKO}.
STRAND 190 194 {ECO:0000244|PDB:1KKO}.
HELIX 200 204 {ECO:0000244|PDB:1KKO}.
HELIX 209 225 {ECO:0000244|PDB:1KKO}.
STRAND 234 238 {ECO:0000244|PDB:1KKO}.
HELIX 242 246 {ECO:0000244|PDB:1KKO}.
TURN 247 249 {ECO:0000244|PDB:1KKO}.
HELIX 251 260 {ECO:0000244|PDB:1KKO}.
HELIX 261 265 {ECO:0000244|PDB:1KKO}.
STRAND 270 273 {ECO:0000244|PDB:1KKO}.
HELIX 281 298 {ECO:0000244|PDB:1KKO}.
STRAND 303 306 {ECO:0000244|PDB:1KKO}.
HELIX 313 321 {ECO:0000244|PDB:1KKO}.
STRAND 326 330 {ECO:0000244|PDB:1KKO}.
HELIX 332 335 {ECO:0000244|PDB:1KKO}.
HELIX 339 351 {ECO:0000244|PDB:1KKO}.
STRAND 354 357 {ECO:0000244|PDB:1KKO}.
HELIX 365 378 {ECO:0000244|PDB:1KKO}.
STRAND 381 384 {ECO:0000244|PDB:1KKO}.
STRAND 389 391 {ECO:0000244|PDB:1KKO}.
HELIX 392 410 {ECO:0000244|PDB:1KKO}.
SEQUENCE 413 AA; 45471 MW; E6101562FDD6DD99 CRC64;
MKIKQALFTA GYSSFYFDDQ QAIKNGAGHD GFIYTGDPVT PGFTSVRQAG ECVSVQLILE
NGAVAVGDCA AVQYSGAGGR DPLFLAEHFI PFLNDHIKPL LEGRDVDAFL PNARFFDKLR
IDGNLLHTAV RYGLSQALLD ATALASGRLK TEVVCDEWQL PCVPEAIPLF GQSGDDRYIA
VDKMILKGVD VLPHALINNV EEKLGFKGEK LREYVRWLSD RILSLRSSPR YHPTLHIDVY
GTIGLIFDMD PVRCAEYIAS LEKEAQGLPL YIEGPVDAGN KPDQIRMLTA ITKELTRLGS
GVKIVADEWC NTYQDIVDFT DAGSCHMVQI KTPDLGGIHN IVDAVLYCNK HGMEAYQGGT
CNETEISART CVHVALAARP MRMLIKPGMG FDEGLNIVFN EMNRTIALLQ TKD


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