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Database: UniProt
Entry: A0A1E4H7B8_9GAMM
LinkDB: A0A1E4H7B8_9GAMM
Original site: A0A1E4H7B8_9GAMM 
ID   A0A1E4H7B8_9GAMM        Unreviewed;       339 AA.
AC   A0A1E4H7B8;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Threonine aldolase {ECO:0000313|EMBL:ODT92140.1};
GN   ORFNames=ABS82_14105 {ECO:0000313|EMBL:ODT92140.1};
OS   Rhodanobacter sp. SCN 67-45.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Rhodanobacter.
OX   NCBI_TaxID=1660133 {ECO:0000313|EMBL:ODT92140.1, ECO:0000313|Proteomes:UP000094158};
RN   [1] {ECO:0000313|EMBL:ODT92140.1, ECO:0000313|Proteomes:UP000094158}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=26031303; DOI=10.1111/1462-2920.12936;
RA   Kantor R.S., van Zyl A.W., van Hille R.P., Thomas B.C., Harrison S.T.,
RA   Banfield J.F.;
RT   "Bioreactor microbial ecosystems for thiocyanate and cyanide degradation
RT   unravelled with genome-resolved metagenomics.";
RL   Environ. Microbiol. 17:4929-4941(2015).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
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:ODT92140.1}.
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DR   EMBL; MEFB01000111; ODT92140.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E4H7B8; -.
DR   Proteomes; UP000094158; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:InterPro.
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; 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;
FT   DOMAIN          5..286
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   339 AA;  36421 MW;  BF63665A3D241196 CRC64;
     MDGVDLRSDT VTRPTAAMRE AMLAAAVGDD VYGEDPTVNA LQQRLADDLG FDAGLFVPSG
     TQSNLLALLA HCERGDEYLV GMDAHTYKFE GGGAAVLGSI QPQPIVQDED GSLPLARIEA
     AIKPVDPHFA RTRLLALENT WHGRPLPLDY LRAARDTARA HGLGLHLDGA RLFNAAVACG
     VPARDLARHF DTVSICLSKG LGAPVGSVLL GSHALIDKAR RWRKVCGGGW RQAGMLAAAG
     MHALDHHVAR LADDHRRAAY LAGRLREIAG IDLLGQHTNM VFVDVPATRL RELDVHLRGA
     GIRISIGYLP TLRLVTHLDV DDDGIERTAA AFAAFFKSH
//
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