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Database: UniProt
Entry: A0A1T4MPL3_9FIRM
LinkDB: A0A1T4MPL3_9FIRM
Original site: A0A1T4MPL3_9FIRM 
ID   A0A1T4MPL3_9FIRM        Unreviewed;       415 AA.
AC   A0A1T4MPL3;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=methylaspartate ammonia-lyase {ECO:0000256|ARBA:ARBA00012993};
DE            EC=4.3.1.2 {ECO:0000256|ARBA:ARBA00012993};
GN   ORFNames=SAMN02745118_01550 {ECO:0000313|EMBL:SJZ68735.1};
OS   Selenihalanaerobacter shriftii.
OC   Bacteria; Bacillota; Clostridia; Halanaerobiales; Halobacteroidaceae;
OC   Selenihalanaerobacter.
OX   NCBI_TaxID=142842 {ECO:0000313|EMBL:SJZ68735.1, ECO:0000313|Proteomes:UP000190625};
RN   [1] {ECO:0000313|Proteomes:UP000190625}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-73 {ECO:0000313|Proteomes:UP000190625};
RA   Varghese N., Submissions S.;
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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         Evidence={ECO:0000256|ARBA:ARBA00000789};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|PIRSR:PIRSR017107-4};
CC   -!- PATHWAY: Amino-acid degradation; L-glutamate degradation via mesaconate
CC       pathway; acetate and pyruvate from L-glutamate: step 2/4.
CC       {ECO:0000256|ARBA:ARBA00004675}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the methylaspartate ammonia-lyase family.
CC       {ECO:0000256|ARBA:ARBA00009954}.
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DR   EMBL; FUWM01000011; SJZ68735.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T4MPL3; -.
DR   STRING; 142842.SAMN02745118_01550; -.
DR   OrthoDB; 8630262at2; -.
DR   UniPathway; UPA00561; UER00618.
DR   Proteomes; UP000190625; Unassembled WGS sequence.
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; Enolase-like C-terminal domain; 1.
DR   Gene3D; 3.30.390.10; Enolase-like, N-terminal domain; 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   NCBIfam; TIGR01502; B_methylAsp_ase; 1.
DR   PANTHER; PTHR48073:SF2; O-SUCCINYLBENZOATE SYNTHASE; 1.
DR   PANTHER; PTHR48073; O-SUCCINYLBENZOATE SYNTHASE-RELATED; 1.
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   SFLD; SFLDG00151; methylaspartate_ammonia-lyase; 1.
DR   SUPFAM; SSF51604; Enolase C-terminal domain-like; 1.
DR   SUPFAM; SSF54826; Enolase N-terminal domain-like; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:SJZ68735.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR017107-4};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR017107-4};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190625}.
FT   DOMAIN          1..159
FT                   /note="Methylaspartate ammonia-lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05034"
FT   DOMAIN          162..410
FT                   /note="Methylaspartate ammonia-lyase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07476"
FT   ACT_SITE        331
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017107-1"
FT   BINDING         172
FT                   /ligand="(2S,3S)-3-methyl-L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:58724"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017107-2"
FT   BINDING         238
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017107-4"
FT   BINDING         273
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017107-4"
FT   BINDING         307
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017107-4"
FT   BINDING         329
FT                   /ligand="(2S,3S)-3-methyl-L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:58724"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017107-2"
FT   SITE            194
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017107-3"
SQ   SEQUENCE   415 AA;  46207 MW;  C40646903EBB9239 CRC64;
     MKIKEIVTSP GLTGFYFDDQ QAIKDGAEHD GVTYIGEAIT EGFTSIRQAG ESISIMIILE
     DGQVAYGDCA AVQYSGAGGR DPLFLAEEFI PIIEEKIGPE LIGKELNSFR ELAEEFDNFK
     VNGKRLHTAI RYGLTQVLLD AVAKAKKKTM TEVVAEEYGL ELSVKPVPIF TQTGDDRYLN
     ADKMIIKHAD VLPHGLINNV KEKLGENGEK LLEYVKWLKD RVEELKNEED YQPIFHIDVY
     GTIGLAFDND PEKMAEYLKG LDEAAQPYTL RIEGPMDSGS RKAQIKDMKA LREEVKKQDI
     DVELVADEWC NTLEDIKMFV DEEAADIVQI KTPDLGGINN TIEAVLYCKE NGVGAYQGGT
     CNETERSAQI CVNLALATRP DQMLAKPGMG VDEGLMIVKN EMERVLSLLR VSQRL
//
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