ID A0A2W1ZT91_9MICO Unreviewed; 336 AA.
AC A0A2W1ZT91;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Low specificity L-threonine aldolase {ECO:0000313|EMBL:PZF58754.1};
GN ORFNames=DEJ23_02815 {ECO:0000313|EMBL:PZF58754.1};
OS Curtobacterium sp. MCSS17_008.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Curtobacterium.
OX NCBI_TaxID=2175647 {ECO:0000313|EMBL:PZF58754.1, ECO:0000313|Proteomes:UP000248620};
RN [1] {ECO:0000313|EMBL:PZF58754.1, ECO:0000313|Proteomes:UP000248620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCSS17_008 {ECO:0000313|EMBL:PZF58754.1,
RC ECO:0000313|Proteomes:UP000248620};
RA Chase A.B., Gomez-Lunar Z., Lopez A.E., Li J., Allison S.D., Martiny A.C.,
RA Martiny J.B.H.;
RT "Emergence of Soil Bacterial Ecotypes Along a Climate Gradient.";
RL Submitted (JUN-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}.
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:PZF58754.1}.
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; QKSM01000002; PZF58754.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W1ZT91; -.
DR OrthoDB; 9774495at2; -.
DR Proteomes; UP000248620; 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;
KW Reference proteome {ECO:0000313|Proteomes:UP000248620}.
FT DOMAIN 7..288
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 204
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ SEQUENCE 336 AA; 35332 MW; 6E2FC3D125975610 CRC64;
MTDAPIDLRS DTVTRPTPAM RRAMAEAEVG DDVFGEDPET NALEQEVADL LGHEAGLFTP
TGSLANQLGL RLHVAPGEEL LADVRAHVVR AELGAAAVFS GITTRTWPSE RGRLVAAAVA
EVAEPNAGAY SVSTTAIAIE NTHNFGGGTV QPVDEVRAVQ AFAREHGIAV HLDGARLWNA
HVASGTPLRE LAEGYDTVSV CLSKGLGAPV GSVLVGSRQH VDAARIWRKR YGGGMRQTGF
LAAAGRHALR YHVDRLAEDH ANARVLAAAL DVDPATVDTN IVFAEVADPP GFVTAAARQG
VRVMQLGPRS VRLVTHLDVS AEDAARAAEV LGALPR
//
