ID I0ALV5_IGNAJ Unreviewed; 342 AA.
AC I0ALV5;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Threonine aldolase {ECO:0000313|EMBL:AFH49962.1};
GN Name=ltaA {ECO:0000313|EMBL:AFH49962.1};
GN OrderedLocusNames=IALB_2259 {ECO:0000313|EMBL:AFH49962.1};
OS Ignavibacterium album (strain DSM 19864 / JCM 16511 / NBRC 101810 /
OS Mat9-16).
OC Bacteria; Ignavibacteriota; Ignavibacteria; Ignavibacteriales;
OC Ignavibacteriaceae; Ignavibacterium.
OX NCBI_TaxID=945713 {ECO:0000313|EMBL:AFH49962.1, ECO:0000313|Proteomes:UP000007394};
RN [1] {ECO:0000313|EMBL:AFH49962.1, ECO:0000313|Proteomes:UP000007394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19864 / JCM 16511 / NBRC 101810 / Mat9-16
RC {ECO:0000313|Proteomes:UP000007394};
RX PubMed=22661972; DOI=10.3389/fmicb.2012.00185;
RA Liu Z., Frigaard N.-U., Vogl K., Iino T., Ohkuma M., Overmann J.,
RA Bryant D.A.;
RT "Complete genome of Ignavibacterium album, a metabolically versatile,
RT flagellated, facultative anaerobe from the phylum Chlorobi.";
RL Front. Microbiol. 3:185-185(2012).
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; CP003418; AFH49962.1; -; Genomic_DNA.
DR RefSeq; WP_014561111.1; NC_017464.1.
DR AlphaFoldDB; I0ALV5; -.
DR STRING; 945713.IALB_2259; -.
DR GeneID; 78243861; -.
DR KEGG; ial:IALB_2259; -.
DR PATRIC; fig|945713.3.peg.2265; -.
DR eggNOG; COG2008; Bacteria.
DR HOGENOM; CLU_029381_0_4_10; -.
DR OrthoDB; 9774495at2; -.
DR Proteomes; UP000007394; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:InterPro.
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 Reference proteome {ECO:0000313|Proteomes:UP000007394}.
FT DOMAIN 5..287
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
FT MOD_RES 202
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ SEQUENCE 342 AA; 37934 MW; 69F5AD506A041A16 CRC64;
MKIIDLRSDT VTKPSQEMRK AMYEAEVGDD VFKEDPTVNK LEEYAAELLG KEAALFVTSG
VMGNQICLNV LTNPGDEVIC ERDAHIFNYE SGSPAKLSGI QLLPVEGKNG VFTSEQVEPL
IRPASAYYMP RTKVIEVENT HNRASGAIWP LEKIIELKNL AKKYNLFYHL DGARIWNASV
ATEISVKEYA SHFDTISCCL SKGLGAPVGS IIAGTKDFIQ EAYRIRKSWG GGMRQAGILA
AAGLYALKNN VERLKEDHEK ARYLAQRISE NKNLEVNLDA VQTNIILFKP LKLSVEEGIK
RCKDEGLILS VGKIDLIRAV THLDVSFDDI KKAADIIDSV FK
//
