ID R4W7C1_9EURY Unreviewed; 449 AA.
AC R4W7C1;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 05-FEB-2025, entry version 49.
DE RecName: Full=methylaspartate ammonia-lyase {ECO:0000256|ARBA:ARBA00012993};
DE EC=4.3.1.2 {ECO:0000256|ARBA:ARBA00012993};
GN ORFNames=L593_04670 {ECO:0000313|EMBL:AGN00883.1};
OS Salinarchaeum sp. Harcht-Bsk1.
OC Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group;
OC Halobacteria; Halobacteriales; Natronoarchaeaceae; Salinarchaeum.
OX NCBI_TaxID=1333523 {ECO:0000313|EMBL:AGN00883.1, ECO:0000313|Proteomes:UP000014072};
RN [1] {ECO:0000313|EMBL:AGN00883.1, ECO:0000313|Proteomes:UP000014072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Harcht-Bsk1 {ECO:0000313|EMBL:AGN00883.1};
RX PubMed=23868130;
RA Dominova I.N., Sorokin D.Y., Kublanov I.V., Patrushev M.V.,
RA Toshchakov S.V.;
RT "Complete Genome Sequence of Salinarchaeum sp. Strain HArcht-Bsk1T,
RT Isolated from Hypersaline Lake Baskunchak, Russia.";
RL Genome Announc. 1:E00505-13(2013).
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; CP005962; AGN00883.1; -; Genomic_DNA.
DR RefSeq; WP_020445777.1; NC_021313.1.
DR AlphaFoldDB; R4W7C1; -.
DR STRING; 1333523.L593_04670; -.
DR GeneID; 16181039; -.
DR KEGG; sali:L593_04670; -.
DR PATRIC; fig|1333523.5.peg.954; -.
DR eggNOG; arCOG06232; Archaea.
DR HOGENOM; CLU_055277_0_0_2; -.
DR OrthoDB; 263744at2157; -.
DR UniPathway; UPA00561; UER00618.
DR Proteomes; UP000014072; 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:AGN00883.1};
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:UP000014072}.
FT DOMAIN 5..164
FT /note="Methylaspartate ammonia-lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF05034"
FT DOMAIN 170..427
FT /note="Methylaspartate ammonia-lyase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07476"
FT REGION 425..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 349
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR017107-1"
FT BINDING 178
FT /ligand="(2S,3S)-3-methyl-L-aspartate"
FT /ligand_id="ChEBI:CHEBI:58724"
FT /evidence="ECO:0000256|PIRSR:PIRSR017107-2"
FT BINDING 254
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR017107-4"
FT BINDING 291
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR017107-4"
FT BINDING 325
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR017107-4"
FT BINDING 347
FT /ligand="(2S,3S)-3-methyl-L-aspartate"
FT /ligand_id="ChEBI:CHEBI:58724"
FT /evidence="ECO:0000256|PIRSR:PIRSR017107-2"
FT SITE 200
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR017107-3"
SQ SEQUENCE 449 AA; 47802 MW; 61FA2C49CCE7E581 CRC64;
MAGNRIVAIR AIPAVSGFYA DDQRAIKRGA TQDGFAYDGE PVTEGFKRIR EAGEALTVEL
ELADGTYATG DCAAVQYSGA GGRDPFFRAE EYRPVVEGPV ADALVGSNPA EFTPLADEIE
SLPAERSGGD RLHTAVRYGV SQALLDAAAK TRGVTKTDVI ADAVGTEPAT QPIPVFGQSG
DDRRTNAEKM LLKRVGVLPH GLFNSVEKVG AEGERLIEYL EWLAVRTDEL GSGASGDENT
QSGVPEYRPR FHVDVYGILG EVFGPPYDRR EVVEYFHRLA DATAPYPLQV EGPMDAGSLS
GQIEQMATLR DALAAADVPV DLVADEWCNT LDDVRAFVDA GAADVVQVKT PDLGGVQRSA
EAVRYCDGTD VRAYLGGTCN ETATSARACA HVALATDAAQ VLAKPGMGFD EGYMLVTNEM
RRALARREHS DSVARPTPET AAPTGDSDD
//
