ID A0A370X410_9GAMM Unreviewed; 338 AA.
AC A0A370X410;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Low-specificity L-threonine aldolase {ECO:0000313|EMBL:RDS82981.1};
DE EC=4.1.2.48 {ECO:0000313|EMBL:RDS82981.1};
GN ORFNames=DWU98_07565 {ECO:0000313|EMBL:RDS82981.1};
OS Dyella monticola.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Dyella.
OX NCBI_TaxID=1927958 {ECO:0000313|EMBL:RDS82981.1, ECO:0000313|Proteomes:UP000254258};
RN [1] {ECO:0000313|EMBL:RDS82981.1, ECO:0000313|Proteomes:UP000254258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4G-K06 {ECO:0000313|EMBL:RDS82981.1,
RC ECO:0000313|Proteomes:UP000254258};
RA Gao Z., Qiu L.;
RT "Dyella monticola sp. nov. and Dyella psychrodurans sp. nov. isolated from
RT monsoon evergreen broad-leaved forest soil of Dinghu Mountain, China.";
RL Submitted (JUL-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 -!- 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:RDS82981.1}.
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DR EMBL; QRBE01000003; RDS82981.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A370X410; -.
DR OrthoDB; 9774495at2; -.
DR Proteomes; UP000254258; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
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; 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 Lyase {ECO:0000313|EMBL:RDS82981.1}.
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 338 AA; 36877 MW; FD846991054D0649 CRC64;
MDWVDLRSDT VTKPTRAMRE AMLNAEVGDD VYGEDPTVNT LQQRLADDLG FEAGLFVPSG
TQSNLLALMS HCERGDEYIV GADAHTYKFE GGGAAVLGSI QPQPIPHDSD GTLSLEKVAA
AIKPVDPHFA RTRLLTLENT WHGRVLPLDY LQAAHDFTRE RTLSLHLDGA RLYNAAIACN
VAAREITSHF DSVSVCLSKG LGAPVGSVLV GSAALIDKAR RWRKVAGGGW RQAGMLAAAC
MHALDHHVAR LADDHARAVR LADGLRDMPG VKLLGQYTNM VFVDVPAERL RELDAHLRAA
SIRISIGYLP TLRLVTHLDV DDAGVERVLD SFRSFFER
//
