ID A0A0W1DEI0_9SPHN Unreviewed; 318 AA.
AC A0A0W1DEI0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Threonine aldolase {ECO:0000313|EMBL:KTE16551.1};
GN ORFNames=ATE71_05170 {ECO:0000313|EMBL:KTE16551.1};
OS Sphingopyxis sp. H115.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=1759073 {ECO:0000313|EMBL:KTE16551.1, ECO:0000313|Proteomes:UP000054021};
RN [1] {ECO:0000313|EMBL:KTE16551.1, ECO:0000313|Proteomes:UP000054021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H115 {ECO:0000313|EMBL:KTE16551.1,
RC ECO:0000313|Proteomes:UP000054021};
RA Zhang Y., Guo Z.;
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:KTE16551.1}.
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DR EMBL; LNSA01000005; KTE16551.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W1DEI0; -.
DR STRING; 1759073.ATE71_05170; -.
DR Proteomes; UP000054021; 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; 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;
FT DOMAIN 1..273
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
SQ SEQUENCE 318 AA; 33569 MW; 845D58AC49E9530B CRC64;
MEALAAANHV DTAYDGDALS QSLDAAFSDL FETTCEVVWI PTGTAANSII LAHFVRPWQG
ILCYEEAHIE VDECGAPTFY SGGAKLMTVP GRGAKIDTEA LKARIAGIRK DVHQVQPAAI
SITNATEYGL AWRAAEIGEI SEIARSSGMK LHMDGARFAN AVAYLDCAPA EVTWRAGVDA
LSFGFTKNGA MMAEAIVFFG GSGGPGVREL KKRGGHLLSK GRFVAAQIRA MLKDDLWLAN
ARAANAGAAK LAAACGSRLM YPVEANELFV RLTAAEAAKL RAAGFDFYDW GEGAARLVVS
WDQDAQAVAP LAAAIGSL
//