ID A9MJL0_SALAR Unreviewed; 413 AA.
AC A9MJL0;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=methylaspartate ammonia-lyase {ECO:0000256|ARBA:ARBA00012993};
DE EC=4.3.1.2 {ECO:0000256|ARBA:ARBA00012993};
GN OrderedLocusNames=SARI_02201 {ECO:0000313|EMBL:ABX22073.1};
OS Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=41514 {ECO:0000313|EMBL:ABX22073.1, ECO:0000313|Proteomes:UP000002084};
RN [1] {ECO:0000313|EMBL:ABX22073.1, ECO:0000313|Proteomes:UP000002084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980
RC {ECO:0000313|Proteomes:UP000002084};
RG The Salmonella enterica serovar Arizonae Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (NOV-2007) 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; CP000880; ABX22073.1; -; Genomic_DNA.
DR AlphaFoldDB; A9MJL0; -.
DR STRING; 41514.SARI_02201; -.
DR KEGG; ses:SARI_02201; -.
DR HOGENOM; CLU_055277_0_0_6; -.
DR UniPathway; UPA00561; UER00618.
DR Proteomes; UP000002084; 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; 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};
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:UP000002084}.
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 413 AA; 45565 MW; 60B75C5A83FB3FAC CRC64;
MKIKQALFTA GYSSFYFDDQ QAIKNGAGHD GFIYTGAPVT PGFTSVRQAG ECVSVQLILE
NGAVAVGDCA AVQYSGAGGR DPLFLAEHFI PFLNNHIKPL LEGRDVDTFL PNARFFDKLR
IDGNLLHTAV RYGLSQALLD ATALATGRLK TEVVYDEWQL PCVPEAIPLF GQSGDDRYIA
VDKMILKGVD VLPHALINNV EEKLGFQGEK LREYVRWLSD RILRLRTSPR YHPTLHIDVY
GTIGLIFDMD PLRCAEYIAS LEKEAQGLPL YIEGPVDAGN KPDQIRLLTA ITKELTRLGS
GVKIVADEWC NTYQDIVDFT DAGSCHMVQI KTPDLGGIHN IVDAVLYCNK HGMEAYQGGT
CNETEISART CVHVALAARP MRMLVKPGMG FDEGLNIVFN EMNRTIALLQ AKD
//
