ID A0A0Q8Z7L8_9ACTN Unreviewed; 356 AA.
AC A0A0Q8Z7L8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Threonine aldolase {ECO:0000313|EMBL:KRD02219.1};
GN ORFNames=ASE41_33930 {ECO:0000313|EMBL:KRD02219.1};
OS Streptomyces sp. Root264.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1736503 {ECO:0000313|EMBL:KRD02219.1, ECO:0000313|Proteomes:UP000051177};
RN [1] {ECO:0000313|EMBL:KRD02219.1, ECO:0000313|Proteomes:UP000051177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root264 {ECO:0000313|EMBL:KRD02219.1,
RC ECO:0000313|Proteomes:UP000051177};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRD02219.1, ECO:0000313|Proteomes:UP000051177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root264 {ECO:0000313|EMBL:KRD02219.1,
RC ECO:0000313|Proteomes:UP000051177};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
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:KRD02219.1}.
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DR EMBL; LMIZ01000051; KRD02219.1; -; Genomic_DNA.
DR RefSeq; WP_057582554.1; NZ_LMIZ01000051.1.
DR AlphaFoldDB; A0A0Q8Z7L8; -.
DR STRING; 1736503.ASE41_33930; -.
DR OrthoDB; 9774495at2; -.
DR Proteomes; UP000051177; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:UniProt.
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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR48097; L-THREONINE ALDOLASE-RELATED; 1.
DR PANTHER; PTHR48097:SF5; LOW SPECIFICITY L-THREONINE ALDOLASE; 1.
DR Pfam; PF01212; Beta_elim_lyase; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000051177}.
FT DOMAIN 19..305
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 356 AA; 38973 MW; E81C13E09AEF4E1D CRC64;
MNPAKTDARR RHDPGVRGFA SDNYAGAHPE VMAALALANG GHQVAYGEDD YTDNLQQIVR
SHFGATAEAF PVFNGTGANV VALQAVTDRW GAVICAESAH INVDEGGAPE RMGGLKLLTV
PTPDGKLTPE LIDRQAWGWE DEHRAMPQVV SITQSTELGT LYTPEEIRAI CDHAHAHGMK
VHLDGSRIAN AAASLDVPMR TFTNAVGVDI LSLGGTKNGA LFGEAVVVID QGAVRRMKHL
RKLSMQLASK MRFVSVQLEA LLAKDLWLRN ARHANEMAQR LAEGVRAVHG VEILYPVQSN
GVFARLPHDV SERLQKKFRF YFWDEAAGVV RWMCAFDTTE EDVDAFVAAL KEEMAR
//
