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Database: UniProt
Entry: A0A1G9TY76_9EURY
LinkDB: A0A1G9TY76_9EURY
Original site: A0A1G9TY76_9EURY 
ID   A0A1G9TY76_9EURY        Unreviewed;       434 AA.
AC   A0A1G9TY76;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=methylaspartate ammonia-lyase {ECO:0000256|ARBA:ARBA00012993};
DE            EC=4.3.1.2 {ECO:0000256|ARBA:ARBA00012993};
GN   ORFNames=SAMN05192554_103197 {ECO:0000313|EMBL:SDM52626.1};
OS   Haloarchaeobius iranensis.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halorubellaceae; Haloarchaeobius.
OX   NCBI_TaxID=996166 {ECO:0000313|EMBL:SDM52626.1, ECO:0000313|Proteomes:UP000199370};
RN   [1] {ECO:0000313|EMBL:SDM52626.1, ECO:0000313|Proteomes:UP000199370}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EB21,IBRC-M 10013,KCTC 4048
RC   {ECO:0000313|Proteomes:UP000199370};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FNIA01000003; SDM52626.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9TY76; -.
DR   STRING; 996166.SAMN05192554_103197; -.
DR   OrthoDB; 263744at2157; -.
DR   UniPathway; UPA00561; UER00618.
DR   Proteomes; UP000199370; 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; SFLDS00001; Enolase; 1.
DR   SFLD; SFLDF00007; 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:SDM52626.1};
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:UP000199370}.
FT   DOMAIN          1..173
FT                   /note="Methylaspartate ammonia-lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05034"
FT   DOMAIN          178..424
FT                   /note="Methylaspartate ammonia-lyase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07476"
FT   ACT_SITE        346
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017107-1"
FT   BINDING         187
FT                   /ligand="(2S,3S)-3-methyl-L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:58724"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017107-2"
FT   BINDING         251
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017107-4"
FT   BINDING         288
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017107-4"
FT   BINDING         322
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017107-4"
FT   BINDING         344
FT                   /ligand="(2S,3S)-3-methyl-L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:58724"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017107-2"
FT   SITE            209
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017107-3"
SQ   SEQUENCE   434 AA;  45817 MW;  E2D37F56F3C8E84B CRC64;
     MRIEAVRAVP TVSGFFFDDQ RAIKDGATQD GFAYDGEPVT PGFDDIREAG EALTVELELE
     DGSVATGDCC AVQYSGAGGR DPLFRAEAYR PVVEGTVAAA LRGRDAAAFA ENASIVEELP
     AERPTDDCGT TGATGDDAGQ LHTAVRYGVS QALLDAAALA ERRTMTETLA DALGTTPATE
     PVPVFGQSGD DRYGNAEKMM IKGVPVLPHG LFNSVEKLGE DGEALREYVD WLATRAVELG
     PDGYEPTIHV DVYGVLGDVL GAPYDRAAVT DYFATLAEAA DPFDVQVEGP MDAGGREEQI
     NDMAELRDGL ASAGVDVDIV ADEWCNTFAD VRAFVDAGAA DLVQVKTPDL GGIQRSAEAV
     RYCEGTDTRA YLGGTCNETV TSARTCAHVA LATDAAQTLA KPGMGFDEGF MVVTNEMRRS
     LARMRPTPEA TADD
//
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