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Database: UniProt
Entry: G2MSI9_9THEO
LinkDB: G2MSI9_9THEO
Original site: G2MSI9_9THEO 
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}.
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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
//
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