ID A0A0G9H5S3_9GAMM Unreviewed; 400 AA.
AC A0A0G9H5S3;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Threonine synthase {ECO:0000313|EMBL:KLD64938.1};
GN ORFNames=Y882_05865 {ECO:0000313|EMBL:KLD64938.1};
OS Dyella japonica DSM 16301.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Dyella.
OX NCBI_TaxID=1440762 {ECO:0000313|EMBL:KLD64938.1, ECO:0000313|Proteomes:UP000035481};
RN [1] {ECO:0000313|EMBL:KLD64938.1, ECO:0000313|Proteomes:UP000035481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16301 {ECO:0000313|EMBL:KLD64938.1,
RC ECO:0000313|Proteomes:UP000035481};
RX PubMed=25481407; DOI=10.1007/s10482-014-0344-8;
RA Naushad S., Adeolu M., Wong S., Sohail M., Schellhorn H.E., Gupta R.S.;
RT "A phylogenomic and molecular marker based taxonomic framework for the
RT order Xanthomonadales: proposal to transfer the families Algiphilaceae and
RT Solimonadaceae to the order Nevskiales ord. nov. and to create a new family
RT within the order Xanthomonadales, the family Rhodanobacteraceae fam. nov.,
RT containing the genus Rhodanobacter and its closest relatives.";
RL Antonie Van Leeuwenhoek 107:467-485(2015).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- PATHWAY: Amino-acid degradation. {ECO:0000256|ARBA:ARBA00005023}.
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:KLD64938.1}.
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DR EMBL; JPLA01000013; KLD64938.1; -; Genomic_DNA.
DR RefSeq; WP_046970919.1; NZ_JPLA01000013.1.
DR AlphaFoldDB; A0A0G9H5S3; -.
DR STRING; 1440762.Y882_05865; -.
DR PATRIC; fig|1440762.4.peg.518; -.
DR OrthoDB; 9778118at2; -.
DR Proteomes; UP000035481; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR CDD; cd01563; Thr-synth_1; 1.
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}.
FT DOMAIN 79..379
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
SQ SEQUENCE 400 AA; 42624 MW; F35A18E2CF2D66B9 CRC64;
MPAIAYLECS RCHARLPADV PQTLCTQCPE QPAGALYVRY DLTPLLGSSP AEAVKGGDAA
TPWRGMWRYR AVLPDVAPVT LGEGWTPMLR SKRHDALFLK EEGANPTGSF KARGLSLAVT
MARHYGLRKL AIPSAGNAAG ALAAYAAASD IEAHIFMPRD VPLANLVEAT AYGAKVTLVD
GVISDCARIV GERKAAEGWF DISTLKEPFR VEGKKTMGYE LVEQLGWEYP DAVFYPTGGG
VGLIGMWKAF DELEQLGWVK PGRRPRMFAI QSSGCAPVVR AFDEGAAVSQ MWKDPKTAAS
GLRVPKAYGD YIILDILRAS GGKAVAVSDE DTFASLRDWA AHEGIFLSPE GAAATAAYDQ
LIASGDLKAS DRVVIFNTGA GLKYTDVIAA ELGLSAAQGP
//
