MAAL1_CARHZ
ID MAAL1_CARHZ Reviewed; 420 AA.
AC Q3AEU2;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Methylaspartate ammonia-lyase 1;
DE Short=MAL;
DE EC=4.3.1.2;
DE AltName: Full=3-methylaspartate ammonia-lyase 1;
DE AltName: Full=Beta-methylaspartase 1;
GN OrderedLocusNames=CHY_0484;
OS Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 /
OS Z-2901).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Carboxydothermus.
OX NCBI_TaxID=246194;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-161 / DSM 6008 / Z-2901;
RX PubMed=16311624; DOI=10.1371/journal.pgen.0010065;
RA Wu M., Ren Q., Durkin A.S., Daugherty S.C., Brinkac L.M., Dodson R.J.,
RA Madupu R., Sullivan S.A., Kolonay J.F., Nelson W.C., Tallon L.J.,
RA Jones K.M., Ulrich L.E., Gonzalez J.M., Zhulin I.B., Robb F.T., Eisen J.A.;
RT "Life in hot carbon monoxide: the complete genome sequence of
RT Carboxydothermus hydrogenoformans Z-2901.";
RL PLoS Genet. 1:563-574(2005).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MASS
RP SPECTROMETRY, SUBSTRATE SPECIFICITY, AND SUBUNIT.
RC STRAIN=ATCC BAA-161 / DSM 6008 / Z-2901;
RX PubMed=22005738; DOI=10.1007/s00253-011-3615-6;
RA Raj H., Puthan Veetil V., Szymanski W., Dekker F.J., Quax W.J.,
RA Feringa B.L., Janssen D.B., Poelarends G.J.;
RT "Characterization of a thermostable methylaspartate ammonia lyase from
RT Carboxydothermus hydrogenoformans.";
RL Appl. Microbiol. Biotechnol. 94:385-397(2012).
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. It can also catalyze the
CC amination of fumarate and ethylfumarate, and the deamination of
CC hydroxylamine, hydrazine, methylamine and ethylamine.
CC {ECO:0000269|PubMed:22005738}.
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:0000269|PubMed:22005738};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.6 mM for mesaconate (at pH 9 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:22005738};
CC KM=4.6 mM for L-threo-beta-methylaspartate (at pH 9 and 30 degrees
CC Celsius) {ECO:0000269|PubMed:22005738};
CC KM=16 mM for L-threo-beta-methylaspartate (at pH 9 and 70 degrees
CC Celsius) {ECO:0000269|PubMed:22005738};
CC Note=kcat is 16 sec(-1) for aminase activity with mesaconate (at pH 9
CC and 30 degrees Celsius). kcat is 16 sec(-1) for deaminase activity
CC with L-threo-beta-methylaspartate (at pH 9 and 30 degrees Celsius).
CC kcat is 78 sec(-1) for deaminase activity with L-threo-beta-
CC methylaspartate (at pH 9 and 70 degrees Celsius).;
CC pH dependence:
CC Optimum pH is 9. {ECO:0000269|PubMed:22005738};
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius. It stays fully active upon
CC incubation at 50 degrees Celsius. Even after 4 hours of incubation,
CC the enzyme retains more than 95% of its initial activity.
CC {ECO:0000269|PubMed:22005738};
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:0000269|PubMed:22005738}.
CC -!- MASS SPECTROMETRY: Mass=49291; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:22005738};
CC -!- SIMILARITY: Belongs to the methylaspartate ammonia-lyase family.
CC {ECO:0000305}.
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DR EMBL; CP000141; ABB16231.1; -; Genomic_DNA.
DR RefSeq; WP_011343418.1; NC_007503.1.
DR AlphaFoldDB; Q3AEU2; -.
DR SMR; Q3AEU2; -.
DR STRING; 246194.CHY_0484; -.
DR EnsemblBacteria; ABB16231; ABB16231; CHY_0484.
DR KEGG; chy:CHY_0484; -.
DR eggNOG; COG3799; Bacteria.
DR HOGENOM; CLU_055277_0_0_9; -.
DR OrthoDB; 254720at2; -.
DR BRENDA; 4.3.1.2; 1178.
DR UniPathway; UPA00561; UER00618.
DR Proteomes; UP000002706; 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; -; 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 1: Evidence at protein level;
KW Lyase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..420
FT /note="Methylaspartate ammonia-lyase 1"
FT /id="PRO_0000429365"
FT ACT_SITE 330
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="(2S,3S)-3-methyl-L-aspartate"
FT /ligand_id="ChEBI:CHEBI:58724"
FT /evidence="ECO:0000250"
FT BINDING 237
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 272
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 306
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 328
FT /ligand="(2S,3S)-3-methyl-L-aspartate"
FT /ligand_id="ChEBI:CHEBI:58724"
FT /evidence="ECO:0000250"
FT BINDING 359..360
FT /ligand="(2S,3S)-3-methyl-L-aspartate"
FT /ligand_id="ChEBI:CHEBI:58724"
FT /evidence="ECO:0000250"
FT SITE 195
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 420 AA; 46398 MW; 76CD7E477E427E8F CRC64;
MRIKDVLFVK GSSGFYFDDQ KAIKSGAVTD GFTYKGKPLT PGFSRVRQGG EAVSIMLFLE
NGEIAVGDCV AVQYSGVDGR DPVFLADNFI EVLEEEIKPR LVGYNLVRFR EAARYFTNLT
DKRGKRYHTA LRYGLTQALL DAVAKINRTT MAEVIAEEYG LDLTLNPVPL FAQSGDDRYI
NADKMILKRV DVLPHGLFNH PAKTGEEGKN LTEYALWLKQ RIKTLGDHDY LPVFHFDVYG
TLGTVFNDNL DRIADYLARL EEKVAPHPLQ IEGPVDLGSK ERQIEGLKYL QEKLITLGSK
VIIVADEWCN NLSDIKEFVD AGAGGMVQIK SPDLGGVNDI IEAVLYAKEK GTGAYLGGSC
NETDVSAKIT VHVGLATGPA QLLVKPGMGV DEGLTIMRNE MMRTLAILQR NKVTFQKKVG
