ID I4DBP3_DESAJ Unreviewed; 416 AA.
AC I4DBP3;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=methylaspartate ammonia-lyase {ECO:0000256|ARBA:ARBA00012993};
DE EC=4.3.1.2 {ECO:0000256|ARBA:ARBA00012993};
GN OrderedLocusNames=Desaci_4373 {ECO:0000313|EMBL:AFM43217.1};
OS Desulfosporosinus acidiphilus (strain DSM 22704 / JCM 16185 / SJ4).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfosporosinus.
OX NCBI_TaxID=646529 {ECO:0000313|EMBL:AFM43217.1, ECO:0000313|Proteomes:UP000002892};
RN [1] {ECO:0000313|EMBL:AFM43217.1, ECO:0000313|Proteomes:UP000002892}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22704 / JCM 16185 / SJ4
RC {ECO:0000313|Proteomes:UP000002892};
RX PubMed=23105050; DOI=10.1128/JB.01392-12;
RA Pester M., Brambilla E., Alazard D., Rattei T., Weinmaier T., Han J.,
RA Lucas S., Lapidus A., Cheng J.F., Goodwin L., Pitluck S., Peters L.,
RA Ovchinnikova G., Teshima H., Detter J.C., Han C.S., Tapia R., Land M.L.,
RA Hauser L., Kyrpides N.C., Ivanova N.N., Pagani I., Huntmann M., Wei C.L.,
RA Davenport K.W., Daligault H., Chain P.S., Chen A., Mavromatis K.,
RA Markowitz V., Szeto E., Mikhailova N., Pati A., Wagner M., Woyke T.,
RA Ollivier B., Klenk H.P., Spring S., Loy A.;
RT "Complete genome sequences of Desulfosporosinus orientis DSM765T,
RT Desulfosporosinus youngiae DSM17734T, Desulfosporosinus meridiei DSM13257T,
RT and Desulfosporosinus acidiphilus DSM22704T.";
RL J. Bacteriol. 194:6300-6301(2012).
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; CP003639; AFM43217.1; -; Genomic_DNA.
DR RefSeq; WP_014829201.1; NC_018068.1.
DR AlphaFoldDB; I4DBP3; -.
DR STRING; 646529.Desaci_4373; -.
DR KEGG; dai:Desaci_4373; -.
DR eggNOG; COG3799; Bacteria.
DR HOGENOM; CLU_055277_0_0_9; -.
DR OrthoDB; 8630262at2; -.
DR UniPathway; UPA00561; UER00618.
DR Proteomes; UP000002892; 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; 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:AFM43217.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR017107-4};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR017107-4}.
FT DOMAIN 1..160
FT /note="Methylaspartate ammonia-lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF05034"
FT DOMAIN 163..411
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 173
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 195
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR017107-3"
SQ SEQUENCE 416 AA; 45474 MW; 20EAE549DD2AFEC7 CRC64;
MKIIDIIASP GLTGFYFDDQ QAIKAGAGHD GFSYTGEPIT PGFKAVRQRG ESISVMLILE
DGQVAAGDCA AVQYSGAGGR DPLFLAEDFI PIILEEIAPK LLGQELNSFR QLVGLVEHSK
RPNGERYHTA IRYGVSQAIL DAVAKAKKKT MTEVILEEYD LPLTLEPVPI FTQTGDDRYD
NADKAIIKRA GVLPHALINN VETKLGANGE LLLDYVIWLR NRILTIGGED YRPVLHIDVY
GTIGIAFKDD TERMVEYFAE LEKAAAPLHL RIEGPMDAGS IDGQIDQLKA LRVALKKRGV
NVEIVADEWC NTYEDIVRFV DAQAADMVQI KTPDLGGIQN TIEAVIYAKK YGVGAYVGGS
CNETDSGGRT AVHVSLAARP DQMLAKPGMG VDEGYMIVHN EMNRTLALLK RKASNR
//
