MAAL2_CARHZ
ID MAAL2_CARHZ Reviewed; 415 AA.
AC Q3AEJ6;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Methylaspartate ammonia-lyase 2;
DE Short=MAL;
DE EC=4.3.1.2;
DE AltName: Full=3-methylaspartate ammonia-lyase 2;
DE AltName: Full=Beta-methylaspartase 2;
GN OrderedLocusNames=CHY_0582;
OS Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 /
OS Z-2901).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Carboxydothermus.
OX NCBI_TaxID=246194;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-161 / DSM 6008 / Z-2901;
RX PubMed=16311624; DOI=10.1371/journal.pgen.0010065;
RA Wu M., Ren Q., Durkin A.S., Daugherty S.C., Brinkac L.M., Dodson R.J.,
RA Madupu R., Sullivan S.A., Kolonay J.F., Nelson W.C., Tallon L.J.,
RA Jones K.M., Ulrich L.E., Gonzalez J.M., Zhulin I.B., Robb F.T., Eisen J.A.;
RT "Life in hot carbon monoxide: the complete genome sequence of
RT Carboxydothermus hydrogenoformans Z-2901.";
RL PLoS Genet. 1:563-574(2005).
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; Evidence={ECO:0000250};
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:0000250}.
CC -!- SIMILARITY: Belongs to the methylaspartate ammonia-lyase family.
CC {ECO:0000305}.
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DR EMBL; CP000141; ABB16209.1; -; Genomic_DNA.
DR RefSeq; WP_011343514.1; NC_007503.1.
DR AlphaFoldDB; Q3AEJ6; -.
DR SMR; Q3AEJ6; -.
DR STRING; 246194.CHY_0582; -.
DR EnsemblBacteria; ABB16209; ABB16209; CHY_0582.
DR KEGG; chy:CHY_0582; -.
DR eggNOG; COG3799; Bacteria.
DR HOGENOM; CLU_055277_0_0_9; -.
DR OMA; RIEGPMD; -.
DR OrthoDB; 254720at2; -.
DR UniPathway; UPA00561; UER00618.
DR Proteomes; UP000002706; Chromosome.
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 3: Inferred from homology;
KW Lyase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..415
FT /note="Methylaspartate ammonia-lyase 2"
FT /id="PRO_0000429366"
FT ACT_SITE 331
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="(2S,3S)-3-methyl-L-aspartate"
FT /ligand_id="ChEBI:CHEBI:58724"
FT /evidence="ECO:0000250"
FT BINDING 238
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 273
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 307
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 329
FT /ligand="(2S,3S)-3-methyl-L-aspartate"
FT /ligand_id="ChEBI:CHEBI:58724"
FT /evidence="ECO:0000250"
FT BINDING 360..361
FT /ligand="(2S,3S)-3-methyl-L-aspartate"
FT /ligand_id="ChEBI:CHEBI:58724"
FT /evidence="ECO:0000250"
FT SITE 195
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 415 AA; 46000 MW; 242CB23BE55D981A CRC64;
MKIIDALFAP GLTGFYFDDQ EAIKKGAVHN GFWYEGNPQT PGYKRIRQKG EAILVMLVLE
NGEVAYGDCA AVQYSGTGGR DPLFTAEEFL PILENEIRPK LIGLELNSFR NLAHIFDREL
TVNGKPLHTA LRYGLTQALL DGVARAQKKL MAEVIAEEYQ LPVIPEPVPI FVQTGDDLYT
NADKAIIKRA DVLPHALINN VEEKLGRQGE KLLAYIKWLK KRIFELAGDE YRPVIHIDVY
GTVGLIFAND LEKIAGYLAT LAHEAAPFKL RIEGPVDMGS LWGQIEALSK LREIIDRRGI
PVEIVADEWC NTLEDIKLFA DHKAGHMVQI KTPDLGGINN VVEAVLYAKM KGIGAYLGGT
CNETDRSAQI SVHLALATRP DQMLAKPGMG LDEGLMIVYN EMQRAIALLK RRGGK
