ID G2MSI9_9THEO Unreviewed; 345 AA.
AC G2MSI9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE SubName: Full=Aromatic amino acid beta-eliminating lyase/threonine aldolase {ECO:0000313|EMBL:AEM77766.1};
GN ORFNames=Thewi_0265 {ECO:0000313|EMBL:AEM77766.1};
OS Thermoanaerobacter wiegelii Rt8.B1.
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacter.
OX NCBI_TaxID=697303 {ECO:0000313|EMBL:AEM77766.1, ECO:0000313|Proteomes:UP000008276};
RN [1] {ECO:0000313|EMBL:AEM77766.1, ECO:0000313|Proteomes:UP000008276}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rt8.B1 {ECO:0000313|EMBL:AEM77766.1,
RC ECO:0000313|Proteomes:UP000008276};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Zeytun A., Daligault H., Detter J.C., Han C.,
RA Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Hemme C.,
RA Woyke T.;
RT "Complete sequence of Thermoanaerobacter wiegelii Rt8.B1.";
RL Submitted (AUG-2011) 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}.
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; CP002991; AEM77766.1; -; Genomic_DNA.
DR RefSeq; WP_014062139.1; NC_015958.1.
DR AlphaFoldDB; G2MSI9; -.
DR STRING; 697303.Thewi_0265; -.
DR KEGG; twi:Thewi_0265; -.
DR eggNOG; COG2008; Bacteria.
DR HOGENOM; CLU_029381_0_4_9; -.
DR Proteomes; UP000008276; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR CDD; cd06502; TA_like; 1.
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; IPR023603; Low_specificity_L-TA-like.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; NF041359; GntG_guanitoxin; 1.
DR PANTHER; PTHR48097:SF9; L-THREONINE ALDOLASE; 1.
DR PANTHER; PTHR48097; L-THREONINE ALDOLASE-RELATED; 1.
DR Pfam; PF01212; Beta_elim_lyase; 1.
DR PIRSF; PIRSF017617; Thr_aldolase; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:AEM77766.1}.
FT DOMAIN 5..288
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
FT MOD_RES 201
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ SEQUENCE 345 AA; 38139 MW; 6429014558CA248A CRC64;
MKYIDLRSDT ITLPTQEMRE AMYKAEVGDD VYGEDPTVRK LEEMAAEMLG KEAAMLVTSG
TQGNQVSIMT HTHPGEEIIV EENCHIITYE VGGVGYLAGV QTKALKSNKG VLNPADVEKA
IRPKDIHYSV TSLICLENTH NRAGGTVTPI EIMKEIYEIA QKHNIPVHLD GARIFNAATY
LNVDVKEIAK YTDSVMFCLS KGLCAPIGSV VVGTKDFIEK ARKYRKMLGG GMRQAGFIAA
AGIVALEKMT KRLQEDHDNA RFLAEGLKNI PGINLDLETV QTNIVMTDIS KTGMTGKEFA
LKLKEHGILI NGGNDFAVRF VTHYYISKKD IEKTLDAIEK IVRQF
//