ID A0A239GRZ1_9ACTN Unreviewed; 425 AA.
AC A0A239GRZ1;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Threonine synthase {ECO:0000313|EMBL:SNS71263.1};
GN ORFNames=SAMN04488107_3525 {ECO:0000313|EMBL:SNS71263.1};
OS Geodermatophilus saharensis.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Geodermatophilus.
OX NCBI_TaxID=1137994 {ECO:0000313|EMBL:SNS71263.1, ECO:0000313|Proteomes:UP000198386};
RN [1] {ECO:0000313|EMBL:SNS71263.1, ECO:0000313|Proteomes:UP000198386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45423 {ECO:0000313|EMBL:SNS71263.1,
RC ECO:0000313|Proteomes:UP000198386};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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; FZOH01000007; SNS71263.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239GRZ1; -.
DR OrthoDB; 9778118at2; -.
DR Proteomes; UP000198386; Unassembled WGS sequence.
DR GO; GO:1901605; P:alpha-amino acid metabolic process; IEA:UniProt.
DR CDD; cd01563; Thr-synth_1; 1.
DR Gene3D; 3.40.50.1100; -; 2.
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; 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.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR604450-51}.
FT DOMAIN 85..392
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 123
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ SEQUENCE 425 AA; 44592 MW; F2A14DE11139CE64 CRC64;
MTLTAPPPTE VPASPARGLV CRNCGATFGL VAEHACAQCF GPLEVDYDPE RMRAVTREQI
EAGPQNIWRY AGLLPVGQDP ADRVSLDPGL TPLVRADRLA AELGITGGLW VKDDSANPTH
SFKDRVVSLA ATAARGLGYA KIAAASTGNL ANSVAAHAAR AGLPSYVFIP ADLEPGKVVQ
SAVYGQTLVA VDGSYDDVNR LTSELAETDE FEDTAFVNQN VRPYYAEGSK TMGYEIAEQL
GWRIPAQVVI PMASGSLLTK VDKAFRELVA AGIAEDTPWR VFGAQSAGCD PIATAFDNGW
DVVKPVKSTG IAKSLNIGNP ADGPYALDAI RRTGGAVGRV GDEQIVQGIR DLARTTGVFA
ETAGGVTVAV LRQLVEDGRL DPAQETVVLN TGEGLKTLDP LTPVVGPTHR IDPSLRSARA
AGLVG
//