ID B0S2T0_FINM2 Unreviewed; 338 AA.
AC B0S2T0;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Low specificity L-threonine aldolase {ECO:0000313|EMBL:BAG08670.1};
GN OrderedLocusNames=FMG_1252 {ECO:0000313|EMBL:BAG08670.1};
OS Finegoldia magna (strain ATCC 29328 / DSM 20472 / WAL 2508)
OS (Peptostreptococcus magnus).
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Finegoldia.
OX NCBI_TaxID=334413 {ECO:0000313|EMBL:BAG08670.1, ECO:0000313|Proteomes:UP000001319};
RN [1] {ECO:0000313|EMBL:BAG08670.1, ECO:0000313|Proteomes:UP000001319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29328 / DSM 20472 / WAL 2508
RC {ECO:0000313|Proteomes:UP000001319};
RX PubMed=18263572; DOI=10.1093/dnares/dsm030;
RA Goto T., Yamashita A., Hirakawa H., Matsutani M., Todo K., Ohshima K.,
RA Toh H., Miyamoto K., Kuhara S., Hattori M., Shimizu T., Akimoto S.;
RT "Complete genome sequence of Finegoldia magna, an anaerobic opportunistic
RT pathogen.";
RL DNA Res. 15:39-47(2008).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the threonine aldolase family.
CC {ECO:0000256|ARBA:ARBA00006966}.
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DR EMBL; AP008971; BAG08670.1; -; Genomic_DNA.
DR RefSeq; WP_012290926.1; NC_010376.1.
DR AlphaFoldDB; B0S2T0; -.
DR STRING; 334413.FMG_1252; -.
DR KEGG; fma:FMG_1252; -.
DR eggNOG; COG2008; Bacteria.
DR HOGENOM; CLU_049619_1_0_9; -.
DR Proteomes; UP000001319; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR001597; ArAA_b-elim_lyase/Thr_aldolase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR48097; L-THREONINE ALDOLASE-RELATED; 1.
DR PANTHER; PTHR48097:SF5; LOW SPECIFICITY L-THREONINE ALDOLASE; 1.
DR Pfam; PF01212; Beta_elim_lyase; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001319}.
FT DOMAIN 14..293
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
SQ SEQUENCE 338 AA; 39203 MW; 7C6B2CBB9843DCE5 CRC64;
MYNFNCDYLE GVHPNIIKAL EETNMVQQQG YCNDEYTHQA KELIKRKISD QDVYFLHGST
ACNKLLIKTS LRPFESVIAC DNAHINTLET GAIEDIGHKI EIVEDEDGLL IPEVIDKFVS
ERMNDPAYFH KPIPKMVYIT NSSESGTIYT KERLMEIRKV CDKHGLYLFM DGARLAYALA
AKNNDLTLKE ICDIVDATYV GGTKCGAMFG EALILNNDEF KLHFKNYIKG SGMLIAKSRF
LGIQFRELFT DDLIFKLAEK ADEQADRIRH RLQEQNYELA TQSTTNTIFV NMDYERYHRL
KHKYNFCENY KTDDYINIRI CTSWSTEEHM VDELIKDL
//
