GenomeNet

Database: UniProt
Entry: A0A0A8X1W3_9BACI
LinkDB: A0A0A8X1W3_9BACI
Original site: A0A0A8X1W3_9BACI 
ID   A0A0A8X1W3_9BACI        Unreviewed;       341 AA.
AC   A0A0A8X1W3;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Low-specificity L-threonine aldolase {ECO:0000313|EMBL:GAM13965.1};
DE            EC=4.1.2.5 {ECO:0000313|EMBL:GAM13965.1};
GN   ORFNames=SAMD00020551_2112 {ECO:0000313|EMBL:GAM13965.1};
OS   Mesobacillus selenatarsenatis SF-1.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Mesobacillus.
OX   NCBI_TaxID=1321606 {ECO:0000313|EMBL:GAM13965.1, ECO:0000313|Proteomes:UP000031014};
RN   [1] {ECO:0000313|EMBL:GAM13965.1, ECO:0000313|Proteomes:UP000031014}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SF-1 {ECO:0000313|EMBL:GAM13965.1,
RC   ECO:0000313|Proteomes:UP000031014};
RA   Kuroda M., Sei K., Yamashita M., Ike M.;
RT   "Whole genome shotgun sequence of Bacillus selenatarsenatis SF-1.";
RL   Submitted (JUN-2013) 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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAM13965.1}.
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; BASE01000044; GAM13965.1; -; Genomic_DNA.
DR   RefSeq; WP_041965768.1; NZ_BASE01000044.1.
DR   AlphaFoldDB; A0A0A8X1W3; -.
DR   STRING; 1321606.SAMD00020551_2112; -.
DR   OrthoDB; 9774495at2; -.
DR   Proteomes; UP000031014; Unassembled WGS sequence.
DR   GO; GO:0004793; F:threonine aldolase activity; IEA:UniProtKB-EC.
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:GAM13965.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031014}.
FT   DOMAIN          3..287
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
FT   MOD_RES         199
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ   SEQUENCE   341 AA;  36877 MW;  3E2EA3ECD9C620A2 CRC64;
     MIDLRSDTVT KPTEEMRKAM YSAEVGDDVY KEDPTVRELE ETAAEILGKE AALFVTSGTQ
     GNQIAVLTHC RPGQELLLEE ESHIFYYESG AVAALAGVQT RTIPGARGAM EPKEVLNAIR
     TEDIHYPETG LICLENTHNR AGGAVVPVEN MEAIYSIALA NKVPVHLDGA RLFNAAAAAG
     VDVKEFAKYT DTVQICLSKG LGAPVGSIIA GNAEFITTAR KWRKRLGGGM RQAGVIAAPG
     LIALTKMKDR LGEDQWNARV LAEAIETIPG MKLARQPETN IVVADVKGLN ITSDVFVERL
     RSEGVISGTF GPTFVRFVTH YDVTEDQIQE AIEAIAKVAR Q
//
DBGET integrated database retrieval system