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}.
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; 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
//