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Database: UniProt
Entry: B1IHF3_CLOBK
LinkDB: B1IHF3_CLOBK
Original site: B1IHF3_CLOBK 
ID   B1IHF3_CLOBK            Unreviewed;       342 AA.
AC   B1IHF3;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   SubName: Full=Putative threonine aldolase {ECO:0000313|EMBL:ACA46644.1};
DE            EC=4.1.2.5 {ECO:0000313|EMBL:ACA46644.1};
GN   OrderedLocusNames=CLD_2342 {ECO:0000313|EMBL:ACA46644.1};
OS   Clostridium botulinum (strain Okra / Type B1).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=498213 {ECO:0000313|EMBL:ACA46644.1, ECO:0000313|Proteomes:UP000008541};
RN   [1] {ECO:0000313|EMBL:ACA46644.1, ECO:0000313|Proteomes:UP000008541}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Okra / Type B1 {ECO:0000313|Proteomes:UP000008541};
RX   PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA   Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA   Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT   "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT   and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT   plasmids.";
RL   PLoS ONE 2:E1271-E1271(2007).
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; CP000939; ACA46644.1; -; Genomic_DNA.
DR   RefSeq; WP_004451603.1; NC_010516.1.
DR   AlphaFoldDB; B1IHF3; -.
DR   KEGG; cbb:CLD_2342; -.
DR   HOGENOM; CLU_049619_1_0_9; -.
DR   Proteomes; UP000008541; Chromosome.
DR   GO; GO:0004793; F:threonine aldolase activity; IEA:UniProtKB-EC.
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:ACA46644.1}.
FT   DOMAIN          17..287
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
SQ   SEQUENCE   342 AA;  38457 MW;  D6FCA16F2E589835 CRC64;
     MYSFKCDYSE GCHPRILKAL AESNITQEEG YGKDSHTKNA ISIIKKLVQN ENVDIHLISG
     GTQTNLISIS SFLRPHEACI CVHSGHIAGP ETGSIEYTGH KVITVDSTNG KITTDKIQQV
     LDFHRNEHFV KPKLVYISNS TEVGTVYTKE EMRNLSEFCK KKNLILYVDG ARLGSALAVK
     ESNLTLKDMC DFSDAFCIGG TKNGALIGEA LVIKNQNLKE DFRYNIKQKG ALLAKGRVLG
     IQFEELFKDN LYFDLANHAN EMASILTKGL KDANCKFFVE SKSNQIFPIL SNENIKILQE
     RFSFNIWEKV DNKNSAIRLV TSWATTKEAV FEFIQELKQL VE
//
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