ID A0A0F7PH70_9EURY Unreviewed; 416 AA.
AC A0A0F7PH70;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Threonine synthase {ECO:0000256|ARBA:ARBA00018679, ECO:0000256|PIRNR:PIRNR038945};
DE EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028, ECO:0000256|PIRNR:PIRNR038945};
GN Name=thrC2 {ECO:0000313|EMBL:AKH98603.1};
GN ORFNames=HLASA_2176 {ECO:0000313|EMBL:ALG83045.1}, HLASF_2142
GN {ECO:0000313|EMBL:AKH98603.1};
OS Halanaeroarchaeum sulfurireducens.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halanaeroarchaeum.
OX NCBI_TaxID=1604004 {ECO:0000313|EMBL:AKH98603.1, ECO:0000313|Proteomes:UP000069906};
RN [1] {ECO:0000313|EMBL:AKH98603.1, ECO:0000313|Proteomes:UP000069906}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HSR2 {ECO:0000313|EMBL:AKH98603.1,
RC ECO:0000313|Proteomes:UP000069906};
RX PubMed=25978546;
RA Sorokin D.Y., Kublanov I.V., Gavrilov S.N., Rojo D., Roman P.,
RA Golyshin P.N., Slepak V.Z., Smedile F., Ferrer M., Messina E., La Cono V.,
RA Yakimov M.M.;
RT "Elemental sulfur and acetate can support life of a novel strictly
RT anaerobic haloarchaeon.";
RL ISME J. 0:0-0(2015).
RN [2] {ECO:0000313|Proteomes:UP000060390}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M27-SA2 {ECO:0000313|Proteomes:UP000060390};
RA Messina E., Kublanov I.V., Toshchakov S., Arcadi E., La Spada G.,
RA La Cono V., Yakimov M.M.;
RT "Complete genome sequence of Halanaeroarchaeum sulfurireducens type strain
RT M27-SA2, a sulfate-reducer haloarchaeon from marine anoxic lake Medee.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ALG83045.1, ECO:0000313|Proteomes:UP000060390}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M27-SA2 {ECO:0000313|EMBL:ALG83045.1,
RC ECO:0000313|Proteomes:UP000060390};
RX PubMed=27182430; DOI=10.1186/s40793-016-0155-9;
RA Messina E., Sorokin D.Y., Kublanov I.V., Toshchakov S., Lopatina A.,
RA Arcadi E., Smedile F., La Spada G., La Cono V., Yakimov M.M.;
RT "Complete genome sequence of 'Halanaeroarchaeum sulfurireducens' M27-SA2, a
RT sulfur-reducing and acetate-oxidizing haloarchaeon from the deep-sea
RT hypersaline anoxic lake Medee.";
RL Stand. Genomic Sci. 11:35-35(2016).
CC -!- FUNCTION: Catalyzes the gamma-elimination of phosphate from L-
CC phosphohomoserine and the beta-addition of water to produce L-
CC threonine. {ECO:0000256|PIRNR:PIRNR038945}.
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 ECO:0000256|PIRNR:PIRNR038945};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRNR:PIRNR038945, ECO:0000256|PIRSR:PIRSR038945-1};
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 5/5. {ECO:0000256|ARBA:ARBA00004979,
CC ECO:0000256|PIRNR:PIRNR038945}.
CC -!- SIMILARITY: Belongs to the threonine synthase family.
CC {ECO:0000256|ARBA:ARBA00005517, ECO:0000256|PIRNR:PIRNR038945}.
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DR EMBL; CP008874; AKH98603.1; -; Genomic_DNA.
DR EMBL; CP011564; ALG83045.1; -; Genomic_DNA.
DR RefSeq; WP_050049253.1; NZ_CP011564.1.
DR AlphaFoldDB; A0A0F7PH70; -.
DR STRING; 1604004.HLASA_2176; -.
DR GeneID; 26011508; -.
DR KEGG; hsf:HLASA_2176; -.
DR KEGG; hsu:HLASF_2142; -.
DR PATRIC; fig|1604004.4.peg.2242; -.
DR HOGENOM; CLU_028142_0_0_2; -.
DR OrthoDB; 6371at2157; -.
DR UniPathway; UPA00050; UER00065.
DR Proteomes; UP000060390; Chromosome.
DR Proteomes; UP000069906; Chromosome.
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; cd01563; Thr-synth_1; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR InterPro; IPR004450; Thr_synthase-like.
DR InterPro; IPR026260; Thr_Synthase_bac/arc.
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 PIRSF; PIRSF038945; Thr_synthase; 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 ECO:0000256|PIRNR:PIRNR038945};
KW Lyase {ECO:0000256|PIRNR:PIRNR038945, ECO:0000313|EMBL:AKH98603.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRNR:PIRNR038945};
KW Reference proteome {ECO:0000313|Proteomes:UP000069906};
KW Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697,
KW ECO:0000256|PIRNR:PIRNR038945}.
FT DOMAIN 79..386
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT BINDING 142
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR038945-1"
FT BINDING 246..250
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR038945-1"
FT BINDING 385
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR038945-1"
FT MOD_RES 116
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR038945-2"
SQ SEQUENCE 416 AA; 43649 MW; 3CABE1312BF57F9E CRC64;
MADLTLSTDT VPDVAEDGVW LTCIECGEAY PPFEDVIYEC AECGGLLEAR YDEYATFEDF
DGEGVWRYAD ALPVSGSVTI DEGNTPLYEA PGIAADVDVA DLRVKHEGMN PTGSFKDRGM
TVGVRVAERL GVDRLVCAST GNTSAALAAY GARSNLETLV LLPAGKVAAG KLAQASLHGA
TILEVDGNFD DCLDIVAELA NMGEAYLLNS LNPFRLEGQK TIGLEMLEQF EADTGDWPDR
IVLPVGNAGN TAALHKAFRE LVEAGAMDDE EVPALTGVQA EGAAPMVEAI ENDYEAVRGW
DDVETRATAI RIGKPVNAPK ALPAIRETGG TAVAVSDDEI TDAQRALAED GIGVEPASAA
SVAGLRKLRD EGVVADDEQV VCLTTGHLLK DPDAAAAAGS EPTQVPNDVD GVLDVL
//
