ID A0A0Q0GE44_9GAMM Unreviewed; 334 AA.
AC A0A0Q0GE44;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Low specificity L-threonine aldolase {ECO:0000313|EMBL:KPZ54795.1};
DE EC=4.1.2.48 {ECO:0000313|EMBL:KPZ54795.1};
GN Name=ltaE {ECO:0000313|EMBL:KPZ54795.1};
GN ORFNames=AN393_02158 {ECO:0000313|EMBL:KPZ54795.1};
OS Pseudoalteromonas sp. P1-25.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=1723758 {ECO:0000313|EMBL:KPZ54795.1, ECO:0000313|Proteomes:UP000050552};
RN [1] {ECO:0000313|EMBL:KPZ54795.1, ECO:0000313|Proteomes:UP000050552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1-25 {ECO:0000313|EMBL:KPZ54795.1,
RC ECO:0000313|Proteomes:UP000050552};
RA Jackson K.R., Lunt B.L., Fisher J.N.B., Gardner A.V., Bailey M.E.,
RA Deus L.M., Earl A.S., Gibby P.D., Hartmann K.A., Liu J.E., Manci A.M.,
RA Nielsen D.A., Solomon M.B., Breakwell D.P., Burnett S.H., Grose J.H.;
RL Submitted (SEP-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 -!- 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:KPZ54795.1}.
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DR EMBL; LKDW01000014; KPZ54795.1; -; Genomic_DNA.
DR RefSeq; WP_055018039.1; NZ_LKDW01000014.1.
DR AlphaFoldDB; A0A0Q0GE44; -.
DR PATRIC; fig|1723758.3.peg.2199; -.
DR OrthoDB; 9774495at2; -.
DR Proteomes; UP000050552; 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:KPZ54795.1}.
FT DOMAIN 3..281
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 197
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ SEQUENCE 334 AA; 36349 MW; 2993182063A9743D CRC64;
MIDFRSDTVT RPSKAMRDAM HNAPVGDDVY GDDPSVNELE AYACERFNFN AALYCSSGTQ
ANLLALMAHC ERGDEYICGQ NAHNYKFEGG GAAVLGSIQP QPIENEKDGS LCFNKIAEAI
KPNDCHFANT RLLSLENTIG GKVLPLEYLA QAHDFVNTHK LALHLDGARA FNAAVDLNVD
ITAITKHFDS VSICLSKGLG APIGSLLLGA PALIDKARRW RKVLGGGMRQ AGMLAAAGQY
ALEHNVNRLQ DDHANARYLA QKLNKLSGFT VDMSNTTNMV YATYSSSINI EELAQALKLQ
GILFSPSKQL RLVTHLDITR EDIDTFLNAL AAHI
//
