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Database: UniProt
Entry: A0A136LI48_9CHLR
LinkDB: A0A136LI48_9CHLR
Original site: A0A136LI48_9CHLR 
ID   A0A136LI48_9CHLR        Unreviewed;       359 AA.
AC   A0A136LI48;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Threonine aldolase {ECO:0000313|EMBL:KXK21335.1};
DE            EC=4.1.2.5 {ECO:0000313|EMBL:KXK21335.1};
GN   ORFNames=UZ15_CFX003001523 {ECO:0000313|EMBL:KXK21335.1};
OS   Chloroflexi bacterium OLB15.
OC   Bacteria; Chloroflexota.
OX   NCBI_TaxID=1617416 {ECO:0000313|EMBL:KXK21335.1, ECO:0000313|Proteomes:UP000070332};
RN   [1] {ECO:0000313|EMBL:KXK21335.1, ECO:0000313|Proteomes:UP000070332}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OLB15 {ECO:0000313|EMBL:KXK21335.1};
RA   Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT   "Genome based microbial ecology of anammox granules in a full-scale
RT   wastewater treatment system.";
RL   Submitted (NOV-2015) 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:KXK21335.1}.
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DR   EMBL; LMZS01000072; KXK21335.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A136LI48; -.
DR   STRING; 1617416.UZ15_CFX003001523; -.
DR   PATRIC; fig|1617416.3.peg.1600; -.
DR   Proteomes; UP000070332; 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:KXK21335.1}.
FT   DOMAIN          5..288
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
FT   MOD_RES         202
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ   SEQUENCE   359 AA;  38761 MW;  AD563BE06D1EDD70 CRC64;
     MNVIDLRSDT VTVPTPAMRE AMANAAVGDD VYGEDPTINE LEATAAEMFG KEAGLFVVSG
     TMGNLTSVLT HCQRGDEFIL GKQSHIFRYE AGSAAMYGGL QPNTLEVQPD GTLILEQIRG
     AIRWDNPHEP VTRLICLENT HGGASGAPVP LAYIEQVAEI AREHNLKLHI DGARIFNAAT
     ALNTDVKTLT APADSVSVCL SKGLCAPVGS VIVGSKDFIK RAHRIRKSLG GGMRQAGILA
     AAGLISLREM STRLAEDHTN ARLLAEGLAA TPYIAVKLEQ VRTNMFFFTL KPDAPITVSD
     LIARLQAEHN IIIRPYNAER GEFRVVTHYW IKQQDVYTVL NAVRSLLGVA VKPIEGAAD
//
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