ID A0A367KVK1_RHIST Unreviewed; 644 AA.
AC A0A367KVK1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=threonine synthase {ECO:0000256|ARBA:ARBA00013028};
DE EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028};
GN Name=THR4 {ECO:0000313|EMBL:RCI05912.1};
GN ORFNames=CU098_010293 {ECO:0000313|EMBL:RCI05912.1};
OS Rhizopus stolonifer (Rhizopus nigricans).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=4846 {ECO:0000313|EMBL:RCI05912.1, ECO:0000313|Proteomes:UP000253551};
RN [1] {ECO:0000313|EMBL:RCI05912.1, ECO:0000313|Proteomes:UP000253551}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LSU 92-RS-03 {ECO:0000313|EMBL:RCI05912.1,
RC ECO:0000313|Proteomes:UP000253551};
RX PubMed=29674435; DOI=10.1534/g3.118.200235;
RA Gryganskyi A.P., Golan J., Dolatabadi S., Mondo S., Robb S., Idnurm A.,
RA Muszewska A., Steczkiewicz K., Masonjones S., Liao H.L., Gajdeczka M.T.,
RA Anike F., Vuek A., Anishchenko I.M., Voigt K., de Hoog G.S., Smith M.E.,
RA Heitman J., Vilgalys R., Stajich J.E.;
RT "Phylogenetic and Phylogenomic Definition of Rhizopus Species.";
RL G3 (Bethesda) 8:2007-2018(2018).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-homoserine = L-threonine + phosphate;
CC Xref=Rhea:RHEA:10840, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57590, ChEBI:CHEBI:57926; EC=4.2.3.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000051};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR604450-51};
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 5/5. {ECO:0000256|ARBA:ARBA00004979}.
CC -!- SIMILARITY: Belongs to the threonine synthase family.
CC {ECO:0000256|ARBA:ARBA00005517}.
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:RCI05912.1}.
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DR EMBL; PJQM01000273; RCI05912.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367KVK1; -.
DR STRING; 4846.A0A367KVK1; -.
DR EnsemblFungi; RCI05912; RCI05912; CU098_010293.
DR UniPathway; UPA00050; UER00065.
DR Proteomes; UP000253551; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0004795; F:threonine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
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.
DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR604450-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000253551};
KW Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697}.
FT DOMAIN 115..193
FT /note="Threonine synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14821"
FT DOMAIN 211..464
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 225
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ SEQUENCE 644 AA; 72222 MW; B7353C9F45514725 CRC64;
MASTYNPSKK KYYIVTSIFS PYKEDINPGS IDSYLFDSRS KAEIFMNKEA KEVYYTQIKS
DEEDYDGNKT PPEEEENDGA FYYANKNCIC FGEDSSMGFS YRRAWGIVKI EEMLYRSTRG
QAKDYTFEDA VMAGLGPDGG LFIPQEIPTL PANWRQAWSQ YSFQQLAVEI LSFYIDETQI
PRADLVQLVE RSYSTFRSKD VTPLAKVHDG LYVLELFHGP TFAFKDVALQ FVGNLFEYFL
ERRNSKEPAG GKTHRLTVVG ATSGDTGSAA IYGLRNKKNV SVFILHPNGR VSPIQEAQMT
TVLDKNVHNL SVEGTFDDCQ DIVKNLFGNK EFNDRHHLGA VNSINWARIL AQTVYYFQAY
FTLLRSLNID PASPEAEAIK FDFSVPTGNF GDVLAGYYAY RMGLPTNKLL IATNENDILY
RFFSSQAYEK QTGPDGGVKA TLSPAMDILV SSNFERLLWY LVRETEADQG KTQDDALNDK
AGQTVAGWMQ ELKEKGVFRV SDAAVLKARE IFDAARVTDV ETSATIRSYY ETNNAGQSPY
VLDPHTAVGV AAAEKLIERD SLKTYPAGSD VLICLATAHP AKFSEAVEAA LKTSPGFDFA
NDVLPTEFHG LLEKERKVTH VERADPQLVI QVIEKELREE GISF
//
