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Database: UniProt
Entry: A0A0N9UAM9_SPHMC
LinkDB: A0A0N9UAM9_SPHMC
Original site: A0A0N9UAM9_SPHMC 
ID   A0A0N9UAM9_SPHMC        Unreviewed;       329 AA.
AC   A0A0N9UAM9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Pyridoxal-5'-phosphate-dependent protein {ECO:0000313|EMBL:ALH80254.1};
GN   ORFNames=AN936_07690 {ECO:0000313|EMBL:ALH80254.1};
OS   Sphingopyxis macrogoltabida (Sphingomonas macrogoltabidus).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=33050 {ECO:0000313|EMBL:ALH80254.1, ECO:0000313|Proteomes:UP000058074};
RN   [1] {ECO:0000313|EMBL:ALH80254.1, ECO:0000313|Proteomes:UP000058074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EY-1 {ECO:0000313|EMBL:ALH80254.1,
RC   ECO:0000313|Proteomes:UP000058074};
RX   PubMed=26634754;
RA   Ohtsubo Y., Nagata Y., Numata M., Tsuchikane K., Hosoyama A., Yamazoe A.,
RA   Tsuda M., Fujita N., Kawai F.;
RT   "Complete Genome Sequence of Polypropylene Glycol- and Polyethylene Glycol-
RT   Degrading Sphingopyxis macrogoltabida Strain EY-1.";
RL   Genome Announc. 3:0-0(2015).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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DR   EMBL; CP012700; ALH80254.1; -; Genomic_DNA.
DR   RefSeq; WP_054587621.1; NZ_CP012700.1.
DR   AlphaFoldDB; A0A0N9UAM9; -.
DR   KEGG; smag:AN936_07690; -.
DR   PATRIC; fig|33050.5.peg.1601; -.
DR   OrthoDB; 9811476at2; -.
DR   Proteomes; UP000058074; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR   InterPro; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   PANTHER; PTHR48078:SF6; ACT DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR48078; THREONINE DEHYDRATASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00291; PALP; 1.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR   PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE   4: Predicted;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000058074}.
FT   DOMAIN          34..315
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
SQ   SEQUENCE   329 AA;  34362 MW;  8C71EAF76B08103F CRC64;
     MTQQSPDPLL DPARAPSLAG VERAAAKVAA LLPQTPLLPI EIDGKTIWCK AECLQPVGAF
     KIRGAWYRLT DLTPEQAAAG VVGVSSGNHA QGVAWAAKRL GIAATIVMPS NAPQMKLAAT
     RALGAEVVLY DRVTESRDAV AAKLLEERGG TLVHAYGDPW IIEGQGTAGV EARAQMQERG
     IDGPDKVIAC CGGGGLSAGL ALALPETELV AVEPEGWDDV KRSLEAGEIL SVEDLAYPTE
     CDALQTPQTW PINFAVLQAR GVRGVVVTRE EVRHAMRVAF EKLHLVVEPG GAAALAAVLA
     GKVELGDATL VTLSGGNVDP KHYAEILAG
//
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