MAAL_HALMA
ID MAAL_HALMA Reviewed; 422 AA.
AC Q5V465;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 11-JUN-2014, sequence version 2.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Methylaspartate ammonia-lyase;
DE Short=MAL;
DE EC=4.3.1.2;
DE AltName: Full=3-methylaspartate ammonia-lyase;
DE AltName: Full=Beta-methylaspartase;
GN Name=mal; OrderedLocusNames=rrnAC0687;
OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS B-1809) (Halobacterium marismortui).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=272569;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=15520287; DOI=10.1101/gr.2700304;
RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA Hood L., Ng W.V.;
RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT Dead Sea.";
RL Genome Res. 14:2221-2234(2004).
RN [2]
RP FUNCTION.
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=21252347; DOI=10.1126/science.1196544;
RA Khomyakova M., Bukmez O., Thomas L.K., Erb T.J., Berg I.A.;
RT "A methylaspartate cycle in haloarchaea.";
RL Science 331:334-337(2011).
CC -!- FUNCTION: Involved in the methylaspartate cycle. Catalyzes the
CC formation of the alpha,beta-unsaturated bond by the reversible anti
CC elimination of ammonia from L-threo-beta-methylaspartate (L-threo-
CC (2S,3S)-3-methylaspartate) to give mesaconate (Probable).
CC {ECO:0000305|PubMed:21252347}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- PATHWAY: Amino-acid degradation; L-glutamate degradation via mesaconate
CC pathway; acetate and pyruvate from L-glutamate: step 2/4.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the methylaspartate ammonia-lyase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAV45687.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY596297; AAV45687.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_049938817.1; NZ_CP039138.1.
DR AlphaFoldDB; Q5V465; -.
DR SMR; Q5V465; -.
DR STRING; 272569.rrnAC0687; -.
DR EnsemblBacteria; AAV45687; AAV45687; rrnAC0687.
DR GeneID; 40151726; -.
DR KEGG; hma:rrnAC0687; -.
DR PATRIC; fig|272569.17.peg.1436; -.
DR eggNOG; arCOG06232; Archaea.
DR HOGENOM; CLU_055277_0_0_2; -.
DR BioCyc; MetaCyc:MON-16255; -.
DR UniPathway; UPA00561; UER00618.
DR Proteomes; UP000001169; Chromosome I.
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; -; 1.
DR Gene3D; 3.30.390.10; -; 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 Pfam; PF07476; MAAL_C; 1.
DR Pfam; PF05034; MAAL_N; 1.
DR PIRSF; PIRSF017107; MAL; 1.
DR SFLD; SFLDF00007; methylaspartate_ammonia-lyase; 1.
DR SUPFAM; SSF51604; SSF51604; 1.
DR SUPFAM; SSF54826; SSF54826; 1.
DR TIGRFAMs; TIGR01502; B_methylAsp_ase; 1.
PE 3: Inferred from homology;
KW Lyase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..422
FT /note="Methylaspartate ammonia-lyase"
FT /id="PRO_0000429368"
FT ACT_SITE 334
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="(2S,3S)-3-methyl-L-aspartate"
FT /ligand_id="ChEBI:CHEBI:58724"
FT /evidence="ECO:0000250"
FT BINDING 239
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 276
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 310
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 332
FT /ligand="(2S,3S)-3-methyl-L-aspartate"
FT /ligand_id="ChEBI:CHEBI:58724"
FT /evidence="ECO:0000250"
FT BINDING 363..364
FT /ligand="(2S,3S)-3-methyl-L-aspartate"
FT /ligand_id="ChEBI:CHEBI:58724"
FT /evidence="ECO:0000250"
FT SITE 197
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 422 AA; 45117 MW; 5CB0F0C697F96EEC CRC64;
MRIEDVRTVP GLSGFFFDDQ QAIKDGATQT GFAYDGQPVT DGFDRIREAG EALIVEIELA
DGSIATGDCA AVQYSGAGGR DPLFRAEKYR PVVEGAVADA LRGQDATQFG ANATMLEEMS
PQRSGGDQLH TAVRYGVSQA LLNAAAQARG VTPTDVLADT YDTEPATSPV PVFGQSGDER
RINAEKMLIK GVPVLPHGLF NSVEKVGENG EGLRDYLAWL SDRATALGPE PYSPRFHVDV
YGILGKVFGP PYDRTEVTDY FETLREAAAP YPLQVEGPMD AGGRQAQITE MAELREGLAD
AGVDVDIVAD EWCNTFEDVQ AFVDAEAADL VQIKTPDLGG IQRSAEAVLY CDGTDTRAYV
GGTCNETVTS ARACAHVALA TDAAQVLAKP GMGFDEGFMV VTNEMRRALA RRDATQEVPA
DD
