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Database: UniProt
Entry: E3DQR4_HALPG
LinkDB: E3DQR4_HALPG
Original site: E3DQR4_HALPG 
ID   E3DQR4_HALPG            Unreviewed;       417 AA.
AC   E3DQR4;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=methylaspartate ammonia-lyase {ECO:0000256|ARBA:ARBA00012993};
DE            EC=4.3.1.2 {ECO:0000256|ARBA:ARBA00012993};
GN   OrderedLocusNames=Hprae_1850 {ECO:0000313|EMBL:ADO77975.1};
OS   Halanaerobium praevalens (strain ATCC 33744 / DSM 2228 / GSL).
OC   Bacteria; Bacillota; Clostridia; Halanaerobiales; Halanaerobiaceae;
OC   Halanaerobium.
OX   NCBI_TaxID=572479 {ECO:0000313|EMBL:ADO77975.1, ECO:0000313|Proteomes:UP000006866};
RN   [1] {ECO:0000313|Proteomes:UP000006866}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33744 / DSM 2228 / GSL
RC   {ECO:0000313|Proteomes:UP000006866};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Ovchinnikova G., Chertkov O., Detter J.C., Han C., Larimer F., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Tindall B., Pomrenke H.G., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Halanaerobium praevalens DSM 2228.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADO77975.1, ECO:0000313|Proteomes:UP000006866}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33744 / DSM 2228 / GSL
RC   {ECO:0000313|Proteomes:UP000006866};
RX   PubMed=21886858;
RA   Ivanova N., Sikorski J., Chertkov O., Nolan M., Lucas S., Hammon N.,
RA   Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA   Huntemann M., Liolios K., Pagani I., Mavromatis K., Ovchinikova G.,
RA   Pati A., Chen A., Palaniappan K., Land M., Hauser L., Brambilla E.M.,
RA   Kannan K.P., Rohde M., Tindall B.J., Goker M., Detter J.C., Woyke T.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P., Lapidus A.;
RT   "Complete genome sequence of the extremely halophilic Halanaerobium
RT   praevalens type strain (GSL).";
RL   Stand. Genomic Sci. 4:312-321(2011).
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; CP002175; ADO77975.1; -; Genomic_DNA.
DR   RefSeq; WP_014553992.1; NC_017455.1.
DR   AlphaFoldDB; E3DQR4; -.
DR   STRING; 572479.Hprae_1850; -.
DR   KEGG; hpk:Hprae_1850; -.
DR   PATRIC; fig|572479.3.peg.1883; -.
DR   eggNOG; COG3799; Bacteria.
DR   HOGENOM; CLU_055277_0_0_9; -.
DR   OrthoDB; 8630262at2; -.
DR   UniPathway; UPA00561; UER00618.
DR   Proteomes; UP000006866; 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:ADO77975.1};
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:UP000006866}.
FT   DOMAIN          1..159
FT                   /note="Methylaspartate ammonia-lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05034"
FT   DOMAIN          163..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   417 AA;  46116 MW;  19C372541E183EF6 CRC64;
     MQIKKVLASK GYTGFYFDDQ AAVKGEAKGD GATYIGKAQT PGFSKVRQAG ESISIMIILE
     NDQIAYGDCA AVQYSGAGGR DPLFLADDFL PVIKAEIAPR LEGREVDNFK ELAAEFDSLK
     INGKRMHTAL RYGITQALLS AVAQAKNKTM AEIVAEEYNL ELDPKPVPVF SQTGDSRHLN
     ADKMIIKQAE VIPHGLINHV EEKLGKNGEK LKEYVNWLKN RIKKIAVDQE YHPAFHLDVY
     GTIGVAFDND PVKMADYLAE LAAEAEPYDL RIEGPMDSGS REAQIKDMKA LKDELARRDI
     KVELVADEWC NTLEDIKLFV DHEAADVVQI KTPDLGGINN TIEAVMYCKE NNVGAYQGGT
     CNETDRSSRI CVNLALATQP DQVLAKPGMG VDEAIMIVKN EMNRILEILK YKDEANK
//
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