ID A0A074YCJ5_AURSE Unreviewed; 567 AA.
AC A0A074YCJ5;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=threonine synthase {ECO:0000256|ARBA:ARBA00013028};
DE EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028};
GN ORFNames=AUEXF2481DRAFT_65660 {ECO:0000313|EMBL:KEQ95465.1};
OS Aureobasidium subglaciale (strain EXF-2481) (Aureobasidium pullulans var.
OS subglaciale).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043005 {ECO:0000313|EMBL:KEQ95465.1, ECO:0000313|Proteomes:UP000030641};
RN [1] {ECO:0000313|EMBL:KEQ95465.1, ECO:0000313|Proteomes:UP000030641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-2481 {ECO:0000313|EMBL:KEQ95465.1,
RC ECO:0000313|Proteomes:UP000030641};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
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}.
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DR EMBL; KL584759; KEQ95465.1; -; Genomic_DNA.
DR RefSeq; XP_013343926.1; XM_013488472.1.
DR AlphaFoldDB; A0A074YCJ5; -.
DR STRING; 1043005.A0A074YCJ5; -.
DR GeneID; 25370122; -.
DR HOGENOM; CLU_015170_1_0_1; -.
DR InParanoid; A0A074YCJ5; -.
DR OMA; FDDCQDM; -.
DR OrthoDB; 275600at2759; -.
DR UniPathway; UPA00050; UER00065.
DR Proteomes; UP000030641; 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:UP000030641};
KW Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697}.
FT DOMAIN 9..88
FT /note="Threonine synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14821"
FT DOMAIN 96..329
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 122
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ SEQUENCE 567 AA; 62358 MW; B61EB036FFDD2827 CRC64;
MSSHTASQRY LSTRGGSYDL SFEDVVLKGL AADGGLFIPE EIPALPSDWQ SKWRNLSFQE
LAFEIFSLYI SDSEIPSADL KDIIHRSYAT FRAKDVTPVV TLDKSKNLHL MELFHGPTFA
FKDVALQFVG NLFEYFLVRM NKGKEGTDRQ HLTVVGATSG DTGSAAIYGL RGKKDVSVFI
MHPKGKVSPV QEAQMTTVLD ANVHNLAVDG TFDDCQDFVK ALFGDADMNS THRLAAVNSI
NWARILAQIT YYFQSYFTLA RSLDTANPTV RFVVPTGNFG DILAGYFAKR MGLPADKLII
ATNENDILHR FWRSGHYEKK PVHGREAEGG FEHDGAKAHS DGVKETLAPA MDILVSSNFE
RLLWYLSYRV NSSDDVTERR KAAGAQVNTW LQALKTDGGF GVEKAILDAA HEDFESERVS
DKQTIDQITE TYASGNGMTP VGENSGAYAT QGTVHQGKYI LDPHSAIGIA ASLRSIQRAP
NAHHIALATA HPAKFSSAVE QALNDQEGFS FAAVQPEQFV GLEQQPRRVT IVKNGAGWQD
VREIVREEVQ LEMEGKASSG PGEIIKG
//
