ID A0A0A7PF42_9SPHN Unreviewed; 336 AA.
AC A0A0A7PF42;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Threonine aldolase {ECO:0000313|EMBL:AJA07853.1};
GN ORFNames=SKP52_04630 {ECO:0000313|EMBL:AJA07853.1};
OS Sphingopyxis fribergensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=1515612 {ECO:0000313|EMBL:AJA07853.1, ECO:0000313|Proteomes:UP000030907};
RN [1] {ECO:0000313|EMBL:AJA07853.1, ECO:0000313|Proteomes:UP000030907}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Kp5.2 {ECO:0000313|EMBL:AJA07853.1,
RC ECO:0000313|Proteomes:UP000030907};
RX PubMed=26040579; DOI=10.1099/ijs.0.000371;
RA Oelschlagel M., Ruckert C., Kalinowski J., Schmidt G., Schlomann M.,
RA Tischler D.;
RT "Description of Sphingopyxis fribergensis sp. nov. - a soil bacterium with
RT the ability to degrade styrene and phenylacetic acid.";
RL Int. J. Syst. Evol. Microbiol. 65:3008-3015(2015).
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}.
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DR EMBL; CP009122; AJA07853.1; -; Genomic_DNA.
DR RefSeq; WP_039572239.1; NZ_CP009122.1.
DR AlphaFoldDB; A0A0A7PF42; -.
DR STRING; 1515612.SKP52_04630; -.
DR KEGG; sphk:SKP52_04630; -.
DR HOGENOM; CLU_049619_0_0_5; -.
DR OrthoDB; 9774495at2; -.
DR Proteomes; UP000030907; Chromosome.
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 6..290
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
SQ SEQUENCE 336 AA; 35453 MW; A2CFE48D235A74CC CRC64;
MTATRFFSDN AATVHPVVME ALAAANHVDT AYDGDALSQS LDAAFSDLFE TTCEVVWIPT
GTAANSIILA HFVRPWQGIL CYEEAHIEVD ECGAPTFYSG GAKLMPLPGR GAKIDTEALK
ARIAGIRRDV HQVQPAAVSI TNATEYGLAW RADEVGAISE ITKGAGMKLH MDGARFANAV
AFLGCAPADV TWRAGVDALS FGFTKNGAMM AEAIVFFGDS GGAGVRELKK RGGHLLSKGR
FVAAQIRAML KDDLWLANAR AANAGAAKLA AACGNRLMYP VEANELFVRL TADEAAQLRG
AGFDFYDWGE GAARLVVSWD QDAEAVAPLA AAIGAL
//
