ID V2XVE3_9FIRM Unreviewed; 342 AA.
AC V2XVE3;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Low specificity L-threonine aldolase {ECO:0000313|EMBL:USF26017.1};
DE EC=4.1.2.48 {ECO:0000313|EMBL:USF26017.1};
GN Name=ltaE {ECO:0000313|EMBL:USF26017.1};
GN ORFNames=N510_000933 {ECO:0000313|EMBL:USF26017.1}, N510_02006
GN {ECO:0000313|EMBL:ESL13609.1};
OS Firmicutes bacterium ASF500.
OC Bacteria; Bacillota.
OX NCBI_TaxID=1378168 {ECO:0000313|EMBL:ESL13609.1};
RN [1] {ECO:0000313|EMBL:ESL13609.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ASF500 {ECO:0000313|EMBL:ESL13609.1};
RX PubMed=24723722;
RA Wannemuehler M.J., Overstreet A.M., Ward D.V., Phillips G.J.;
RT "Draft genome sequences of the altered schaedler flora, a defined bacterial
RT community from gnotobiotic mice.";
RL Genome Announc. 2:e00287-e00214(2014).
RN [2] {ECO:0000313|EMBL:USF26017.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ASF500 {ECO:0000313|EMBL:USF26017.1};
RA Proctor A., Parvinroo S., Richie T., Jia X., Lee S.T.M., Karp P.D.,
RA Paley S., Kostic A.D., Pierre J.F., Wannemuehler M.J., Phillips G.J.;
RT "Resources to Facilitate Use of the Altered Schaedler Flora (ASF) Mouse
RT Model to Study Microbiome Function.";
RL Submitted (MAY-2022) to the EMBL/GenBank/DDBJ databases.
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; AYJP01000008; ESL13609.1; -; Genomic_DNA.
DR EMBL; CP097573; USF26017.1; -; Genomic_DNA.
DR AlphaFoldDB; V2XVE3; -.
DR STRING; 1378168.N510_02006; -.
DR PATRIC; fig|1378168.3.peg.2084; -.
DR eggNOG; COG2008; Bacteria.
DR HOGENOM; CLU_049619_1_0_9; -.
DR OrthoDB; 9774495at2; -.
DR Proteomes; UP000017395; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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 Lyase {ECO:0000313|EMBL:USF26017.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000017395}.
FT DOMAIN 7..241
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
SQ SEQUENCE 342 AA; 37444 MW; 2AB2DFE70D2FD36B CRC64;
MIRFECDYTT GAHPKILEAL VNTNGEACPG YGVDDHCERA RDMLRGLCQA PDAGVHFLVG
GTQANATIIA AALRPHQGVL CAETGHINVH ETGAIEATGH KVLGLPAAEG KITPQQIHDY
CEAHHSNPAW EHMVQPGMVY LSLPTELGTV YTLAELEAIH EICQRWRLPL FVDGARLACG
LAASDVTLPD LARLCDVFYL GGTKAGLLFG EAVVITNPNL DHDFRYLIKQ HGGMLAKGRL
LGVQFEAFLT DGLFFEIGKK EVAQAMRLRA AFLEKGYPLF VSSASNQQFP VLPDGHMLAL
EKKYSFEFWE KVDSTHTAVR FCTSWSTTDE DVDALIADIR AL
//
