ID A0A0F4YJX7_TALEM Unreviewed; 998 AA.
AC A0A0F4YJX7;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, 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=T310_8163 {ECO:0000313|EMBL:KKA17898.1};
OS Rasamsonia emersonii CBS 393.64.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX NCBI_TaxID=1408163 {ECO:0000313|EMBL:KKA17898.1, ECO:0000313|Proteomes:UP000053958};
RN [1] {ECO:0000313|EMBL:KKA17898.1, ECO:0000313|Proteomes:UP000053958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 393.64 {ECO:0000313|EMBL:KKA17898.1,
RC ECO:0000313|Proteomes:UP000053958};
RA Heijne W.H., Fedorova N.D., Nierman W.C., Vollebregt A.W., Zhao Z., Wu L.,
RA Kumar M., Stam H., van den Berg M.A., Pel H.J.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU361277};
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 -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|RuleBase:RU361277}.
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:KKA17898.1}.
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DR EMBL; LASV01000532; KKA17898.1; -; Genomic_DNA.
DR RefSeq; XP_013324510.1; XM_013469056.1.
DR AlphaFoldDB; A0A0F4YJX7; -.
DR STRING; 1408163.A0A0F4YJX7; -.
DR GeneID; 25320423; -.
DR OrthoDB; 275600at2759; -.
DR UniPathway; UPA00050; UER00065.
DR Proteomes; UP000053958; Unassembled WGS sequence.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0004795; F:threonine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd05283; CAD1; 1.
DR CDD; cd01560; Thr-synth_2; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.90.1380.10; Threonine synthase, N-terminal domain; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR047109; CAD-like.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
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; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR Pfam; PF00291; PALP; 1.
DR Pfam; PF14821; Thr_synth_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR PROSITE; PS00059; ADH_ZINC; 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 Metal-binding {ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR604450-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000053958};
KW Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 21..356
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
FT MOD_RES 580
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ SEQUENCE 998 AA; 109915 MW; 5A0C34FF56F72202 CRC64;
MSATDYKFEG WLGLDASSAE GKMVWKEFEP KPWEETDVDI KITHCGICGS DLHTLRSGWA
PTNYPCCVGH EIVGIAVRVG SQVSHVKVGD RVGVGAQADS CLGRKGDCEE CAMGKEAYCM
KHFVPTYNGN HLNGAKSMGG YALYNRSPGH FVFKIPDAIP SEEAAPMLCG GVTVWSPLKQ
NGCGPGKKVG VVGVGGLGHF AVLFAKALGA DKVVAISRRA SKAADALKLG ADVYIATEDE
PDWAKTHARS LDLIICTVSS DKMPINDYLS LLRYGGHFIQ VGLPDAGVLG MPVFTVLRSN
LKIGGTFIGS PHEIREMLDF VAEKGIHPWV EQRSMKDANQ AIVDMEKGRA RYRYVLVNEQ
HLLIEEYSVR SIVVRFPVST WRDRWTNQSA VERRRCRHAL SPIGTRGMRR RSHAPEISWQ
TCVSPPAGLR RSSLFSDAVQ SVSDFTDLPS IELLSIENHL ANDASSLATL PQHEGFRLSF
EDVVLKGLAS DGGLFVPEQI PSVPASWESD WRNLSFEDLA FQIVSLYVSP SEIPPEDLKD
IIRRSYSTFR HPERTPLVEL DRTRNLYLLE LFHGPTFAFK DVALQFLGNL FEYFLVRKNQ
GKQGKDRHHL TVIGATSGDT GSAAIYGLRG KKDVSIFILF PKGRVSPIQQ AQMTTVLDSN
VHNLTVEGSF DDCQDIVKSL FADPDLNSTH NVAAVNSINW ARILAQMTYY FYSYFTLTKS
PGFQQGSKVR FVVPSGNFGD ILAGWFAKRM GLPAEKLVIA TNENDILDRF FKSGGHYTKS
PLNGPAAQGV KETHSPAMDI LVSSNFERLL WFLTFEADGS ASVDERRRNA SERIRTWLNE
LKTQGGFSVT EAVFEGAKRE FESERVSDEQ TIETIRAIYT SCFPPNLGRG SAHSSKTGGY
ILDPHSAVGV AASLRSVERN PGTSHISLST AHPAKFANAV DLALRGQDGY DFAEVLPQEF
VGLEQKESRV TPVGAGVGWQ GVREIVKAEV EQELQGLR
//
