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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//