ID A1VPG0_POLNA Unreviewed; 475 AA.
AC A1VPG0;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=L-threonine synthase {ECO:0000313|EMBL:ABM37538.1};
DE EC=4.2.3.1 {ECO:0000313|EMBL:ABM37538.1};
GN OrderedLocusNames=Pnap_2230 {ECO:0000313|EMBL:ABM37538.1};
OS Polaromonas naphthalenivorans (strain CJ2).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=365044 {ECO:0000313|EMBL:ABM37538.1, ECO:0000313|Proteomes:UP000000644};
RN [1] {ECO:0000313|Proteomes:UP000000644}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CJ2 {ECO:0000313|Proteomes:UP000000644};
RX PubMed=19453698; DOI=10.1111/j.1462-2920.2009.01947.x;
RA Yagi J.M., Sims D., Brettin T., Bruce D., Madsen E.L.;
RT "The genome of Polaromonas naphthalenivorans strain CJ2, isolated from coal
RT tar-contaminated sediment, reveals physiological and metabolic versatility
RT and evolution through extensive horizontal gene transfer.";
RL Environ. Microbiol. 11:2253-2270(2009).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR604450-51};
CC -!- SIMILARITY: Belongs to the threonine synthase family.
CC {ECO:0000256|ARBA:ARBA00005517}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000529; ABM37538.1; -; Genomic_DNA.
DR RefSeq; WP_011801616.1; NC_008781.1.
DR AlphaFoldDB; A1VPG0; -.
DR STRING; 365044.Pnap_2230; -.
DR KEGG; pna:Pnap_2230; -.
DR eggNOG; COG0498; Bacteria.
DR HOGENOM; CLU_015170_1_0_4; -.
DR OrthoDB; 9763107at2; -.
DR Proteomes; UP000000644; Chromosome.
DR GO; GO:0004795; F:threonine synthase activity; IEA:UniProtKB-EC.
DR CDD; cd01560; Thr-synth_2; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR Gene3D; 3.90.1380.10; Threonine synthase, N-terminal domain; 1.
DR InterPro; IPR029144; Thr_synth_N.
DR InterPro; IPR037158; Thr_synth_N_sf.
DR InterPro; IPR004450; Thr_synthase-like.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR NCBIfam; TIGR00260; thrC; 1.
DR PANTHER; PTHR42690; THREONINE SYNTHASE FAMILY MEMBER; 1.
DR PANTHER; PTHR42690:SF1; THREONINE SYNTHASE-LIKE 2; 1.
DR Pfam; PF00291; PALP; 1.
DR Pfam; PF14821; Thr_synth_N; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:ABM37538.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR604450-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000000644}.
FT DOMAIN 2..83
FT /note="Threonine synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14821"
FT DOMAIN 93..339
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 117
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ SEQUENCE 475 AA; 52312 MW; CA85DDE6E9C18B0A CRC64;
MHYISTRASS GNAPERKRFC EILLEGLAPD GGLYLPEYYP QVSDATLTAW RGLSYAELAF
EVLSLYIDDI PAADLKAICD KTYTEEVFGT QEIVPLRPLE SGLYLEALSN GPTLAFKDMA
MQLLGNLFEY ELARRGEELN ILGATSGDTG SAAEYAMRGK KGVRVFMTSP NGRMSPFQQA
QMFSLQDENI HNIAIDGVFD DCQDIVKAVS NDLAFKRQYK IGTVNSINWA RLMAQVVYYF
AGYFQATRTN AEKVSFTVPS GNFGNVCAGH VARSMGLPIA QLVVATNEND VLDEFFRTGI
YRVRTSADTH ETSSPSMDIS KASNFERFVF DLLGRDGGKT RALFHDQLNS QGSFELGADP
AFAMAAERYG FVSGKSTHAD RLATIRDTYQ RFGTMIDTHT ADGVKVAREH VQPGVPMIVL
ETALPIKFAA TIEEALGQPP ARPARFEGIE ALPKRVKLLP ADAAVIKRYI AENVH
//
