ID A0A2I8DE08_9BURK Unreviewed; 352 AA.
AC A0A2I8DE08;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Threonine aldolase {ECO:0000313|EMBL:AUT45412.1};
GN ORFNames=C2U31_05115 {ECO:0000313|EMBL:AUT45412.1};
OS Achromobacter sp. AONIH1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=1758194 {ECO:0000313|EMBL:AUT45412.1, ECO:0000313|Proteomes:UP000236176};
RN [1] {ECO:0000313|Proteomes:UP000236176}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AONIH1 {ECO:0000313|Proteomes:UP000236176};
RX PubMed=29437920;
RG NISC Comparative Sequencing Program;
RA Weingarten R.A., Johnson R.C., Conlan S., Ramsburg A.M., Dekker J.P.,
RA Lau A.F., Khil P., Odom R.T., Deming C., Park M., Thomas P.J.,
RA Henderson D.K., Palmore T.N., Segre J.A., Frank K.M.;
RT "Genomic Analysis of Hospital Plumbing Reveals Diverse Reservoir of
RT Bacterial Plasmids Conferring Carbapenem Resistance.";
RL MBio 9:e02011-e02017(2018).
RN [2] {ECO:0000313|Proteomes:UP000236176}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AONIH1 {ECO:0000313|Proteomes:UP000236176};
RA Segre J.A., Mullikin J.;
RL Submitted (JAN-2018) 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}.
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DR EMBL; CP026124; AUT45412.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I8DE08; -.
DR KEGG; achr:C2U31_05115; -.
DR OrthoDB; 9774495at2; -.
DR Proteomes; UP000236176; Chromosome.
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;
KW Reference proteome {ECO:0000313|Proteomes:UP000236176}.
FT DOMAIN 15..296
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
FT MOD_RES 209
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ SEQUENCE 352 AA; 37267 MW; FB2DDB1B87976E3B CRC64;
MTEQTFAPRP ANAVDLRSDT VTLPTEAMYE RMRGAPIGDD ALDGDPTVRE LEAYVAAQLG
KQAGLFVPSC TMANLLAVLA QTQRNEQVIL ESTAHMYTSE RGAATFTGVF YHCVPGADGA
MDLNRLEEAL LTEGMRLKTS LVAMETTHNN AGGTVLPLDH MRSVYGMANS RGISVHLDGA
RMYNAAVALG VTPLDIAQHA DTVSLCLSKG LSAPVGAVLA GPRPLLAKAR TLRRMLGGAQ
RQAGIMGAAG LEAVQTMGGR LAEDHATAAR LSEGLNRLHP RLSATVPQTN IVQVETADSG
MGNAQWVQAL AAEGVLTRPW GVTRLRCVTH RHIGAADIDR AVQAFGRVLQ AS
//
