ID U4Q7R5_TEPAE Unreviewed; 242 AA.
AC U4Q7R5;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=methylaspartate ammonia-lyase {ECO:0000256|ARBA:ARBA00012993};
DE EC=4.3.1.2 {ECO:0000256|ARBA:ARBA00012993};
GN OrderedLocusNames=TEPIRE1_0120 {ECO:0000313|EMBL:CDI40290.1};
OS Tepidanaerobacter acetatoxydans (strain DSM 21804 / JCM 16047 / Re1).
OC Bacteria; Bacillota; Clostridia; Thermosediminibacterales;
OC Tepidanaerobacteraceae; Tepidanaerobacter.
OX NCBI_TaxID=1209989 {ECO:0000313|EMBL:CDI40290.1, ECO:0000313|Proteomes:UP000010802};
RN [1] {ECO:0000313|Proteomes:UP000010802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Re1 {ECO:0000313|Proteomes:UP000010802};
RX PubMed=23469343; DOI=10.1128/genomeA.00213-12;
RA Manzoor S., Bongcam-Rudloff E., Schnurer A., Muller B.;
RT "First genome sequence of a syntrophic acetate-oxidizing bacterium,
RT Tepidanaerobacter acetatoxydans strain Re1.";
RL Genome Announc. 1:E00213-E00213(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 -!- 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HF563609; CDI40290.1; -; Genomic_DNA.
DR AlphaFoldDB; U4Q7R5; -.
DR STRING; 1209989.TepRe1_0115; -.
DR KEGG; tae:TepiRe1_0120; -.
DR eggNOG; COG3799; Bacteria.
DR HOGENOM; CLU_100237_0_0_9; -.
DR UniPathway; UPA00561; UER00618.
DR Proteomes; UP000010802; 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 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 Pfam; PF07476; MAAL_C; 1.
DR Pfam; PF05034; MAAL_N; 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:CDI40290.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000010802}.
FT DOMAIN 10..167
FT /note="Methylaspartate ammonia-lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF05034"
FT DOMAIN 173..241
FT /note="Methylaspartate ammonia-lyase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07476"
SQ SEQUENCE 242 AA; 26912 MW; 0883C3A674F69E8B CRC64;
MHEGDKAMSK IKEVIASKGL AGFYFDDQAA IKSDAKEDGF IYKGTPKTKG FTDVRQAGES
ISVMIITDDG KMAYGDCAAV QYSGAGGRDP LFLAEDFIPV IENEIRPILI GEELDSFRRL
ADKIDSYKID GKSLHTALRY GITQAILDAV AKAKNTTRTE VVAEEYGLEL ELIPVPIFAQ
SGDDRYTNAD KMIIKRVDVL PHALINNVSK LGKQGEKLIE YINWLKQRIY QIAGDDYKPY
FT
//
