MAAL_CITAM
ID MAAL_CITAM Reviewed; 413 AA.
AC O66145;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Methylaspartate ammonia-lyase;
DE Short=MAL;
DE EC=4.3.1.2;
DE AltName: Full=3-methylaspartate ammonia-lyase;
DE AltName: Full=Beta-methylaspartase;
OS Citrobacter amalonaticus.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=35703;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=YG-1002;
RX PubMed=9830098; DOI=10.1007/s002530051322;
RA Kato Y., Asano Y.;
RT "Cloning, nucleotide sequencing, and expression of the 3-methylaspartate
RT ammonia-lyase gene from Citrobacter amalonaticus strain YG-1002.";
RL Appl. Microbiol. Biotechnol. 50:468-474(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.33 ANGSTROMS) IN COMPLEX WITH
RP L-THREO-BETA-METHYLASPARTATE AND MAGNESIUM, ACTIVE SITE, COFACTOR, AND
RP SUBUNIT.
RX PubMed=11796115; DOI=10.1016/s0969-2126(01)00696-7;
RA Levy C.W., Buckley P.A., Sedelnikova S., Kato Y., Asano Y., Rice D.W.,
RA Baker P.J.;
RT "Insights into enzyme evolution revealed by the structure of
RT methylaspartate ammonia lyase.";
RL Structure 10:105-113(2002).
CC -!- FUNCTION: Involved in the methylaspartate cycle. Catalyzes the
CC formation of the alpha,beta-unsaturated bond by the reversible anti
CC elimination of ammonia from L-threo-beta-methylaspartate (L-threo-
CC (2S,3S)-3-methylaspartate) to give mesaconate (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S,3S)-3-methyl-L-aspartate = mesaconate + NH4(+);
CC Xref=Rhea:RHEA:12829, ChEBI:CHEBI:28938, ChEBI:CHEBI:36986,
CC ChEBI:CHEBI:58724; EC=4.3.1.2;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:11796115};
CC -!- PATHWAY: Amino-acid degradation; L-glutamate degradation via mesaconate
CC pathway; acetate and pyruvate from L-glutamate: step 2/4.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11796115}.
CC -!- SIMILARITY: Belongs to the methylaspartate ammonia-lyase family.
CC {ECO:0000305}.
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DR EMBL; AB005294; BAA28709.1; -; Genomic_DNA.
DR PIR; T43810; T43810.
DR PDB; 1KKO; X-ray; 1.33 A; A/B=1-413.
DR PDB; 1KKR; X-ray; 2.10 A; A/B=1-413.
DR PDBsum; 1KKO; -.
DR PDBsum; 1KKR; -.
DR AlphaFoldDB; O66145; -.
DR SMR; O66145; -.
DR STRING; 35703.DQ02_11510; -.
DR DrugBank; DB04538; threo-3-methyl-L-aspartic acid.
DR GeneID; 67372035; -.
DR eggNOG; COG3799; Bacteria.
DR UniPathway; UPA00561; UER00618.
DR EvolutionaryTrace; O66145; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050096; F:methylaspartate ammonia-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0019553; P:glutamate catabolic process via L-citramalate; IEA:UniProtKB-UniPathway.
DR CDD; cd03314; MAL; 1.
DR Gene3D; 3.20.20.120; -; 1.
DR Gene3D; 3.30.390.10; -; 1.
DR InterPro; IPR036849; Enolase-like_C_sf.
DR InterPro; IPR029017; Enolase-like_N.
DR InterPro; IPR006395; Me_Asp_am_lyase.
DR InterPro; IPR022662; MeAsp_NH4-lyase_C.
DR InterPro; IPR022665; MeAsp_NH4-lyase_N.
DR Pfam; PF07476; MAAL_C; 1.
DR Pfam; PF05034; MAAL_N; 1.
DR PIRSF; PIRSF017107; MAL; 1.
DR SFLD; SFLDF00007; methylaspartate_ammonia-lyase; 1.
DR SUPFAM; SSF51604; SSF51604; 1.
DR SUPFAM; SSF54826; SSF54826; 1.
DR TIGRFAMs; TIGR01502; B_methylAsp_ase; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lyase; Magnesium; Metal-binding.
FT CHAIN 1..413
FT /note="Methylaspartate ammonia-lyase"
FT /id="PRO_0000429367"
FT ACT_SITE 331
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:11796115"
FT BINDING 172
FT /ligand="(2S,3S)-3-methyl-L-aspartate"
FT /ligand_id="ChEBI:CHEBI:58724"
FT /evidence="ECO:0000269|PubMed:11796115"
FT BINDING 238
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:11796115"
FT BINDING 273
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:11796115"
FT BINDING 307
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:11796115"
FT BINDING 329
FT /ligand="(2S,3S)-3-methyl-L-aspartate"
FT /ligand_id="ChEBI:CHEBI:58724"
FT /evidence="ECO:0000269|PubMed:11796115"
FT BINDING 360..361
FT /ligand="(2S,3S)-3-methyl-L-aspartate"
FT /ligand_id="ChEBI:CHEBI:58724"
FT SITE 194
FT /note="Transition state stabilizer"
FT STRAND 2..18
FT /evidence="ECO:0007829|PDB:1KKO"
FT HELIX 20..24
FT /evidence="ECO:0007829|PDB:1KKO"
FT STRAND 44..59
FT /evidence="ECO:0007829|PDB:1KKO"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:1KKO"
FT TURN 73..76
FT /evidence="ECO:0007829|PDB:1KKO"
FT HELIX 86..96
FT /evidence="ECO:0007829|PDB:1KKO"
FT HELIX 98..101
FT /evidence="ECO:0007829|PDB:1KKO"
FT HELIX 110..118
FT /evidence="ECO:0007829|PDB:1KKO"
FT HELIX 128..145
FT /evidence="ECO:0007829|PDB:1KKO"
FT HELIX 150..157
FT /evidence="ECO:0007829|PDB:1KKO"
FT HELIX 179..186
FT /evidence="ECO:0007829|PDB:1KKO"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:1KKO"
FT HELIX 200..204
FT /evidence="ECO:0007829|PDB:1KKO"
FT HELIX 209..225
FT /evidence="ECO:0007829|PDB:1KKO"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:1KKO"
FT HELIX 242..246
FT /evidence="ECO:0007829|PDB:1KKO"
FT TURN 247..249
FT /evidence="ECO:0007829|PDB:1KKO"
FT HELIX 251..260
FT /evidence="ECO:0007829|PDB:1KKO"
FT HELIX 261..265
FT /evidence="ECO:0007829|PDB:1KKO"
FT STRAND 270..273
FT /evidence="ECO:0007829|PDB:1KKO"
FT HELIX 281..298
FT /evidence="ECO:0007829|PDB:1KKO"
FT STRAND 303..306
FT /evidence="ECO:0007829|PDB:1KKO"
FT HELIX 313..321
FT /evidence="ECO:0007829|PDB:1KKO"
FT STRAND 326..330
FT /evidence="ECO:0007829|PDB:1KKO"
FT HELIX 332..335
FT /evidence="ECO:0007829|PDB:1KKO"
FT HELIX 339..351
FT /evidence="ECO:0007829|PDB:1KKO"
FT STRAND 354..357
FT /evidence="ECO:0007829|PDB:1KKO"
FT HELIX 365..378
FT /evidence="ECO:0007829|PDB:1KKO"
FT STRAND 381..384
FT /evidence="ECO:0007829|PDB:1KKO"
FT STRAND 389..391
FT /evidence="ECO:0007829|PDB:1KKO"
FT HELIX 392..410
FT /evidence="ECO:0007829|PDB:1KKO"
SQ 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
