ID F7PNU2_9EURY Unreviewed; 423 AA.
AC F7PNU2;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 58.
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=thrC1 {ECO:0000313|EMBL:ERJ06750.1};
GN ORFNames=HLRTI_001166 {ECO:0000313|EMBL:ERJ06750.1}, HTIA_1546
GN {ECO:0000313|EMBL:CCQ33673.1};
OS Halorhabdus tiamatea SARL4B.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Halorhabdus.
OX NCBI_TaxID=1033806 {ECO:0000313|EMBL:ERJ06750.1, ECO:0000313|Proteomes:UP000003861};
RN [1] {ECO:0000313|EMBL:ERJ06750.1, ECO:0000313|Proteomes:UP000003861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SARL4B {ECO:0000313|EMBL:ERJ06750.1,
RC ECO:0000313|Proteomes:UP000003861};
RX PubMed=21705593; DOI=10.1128/JB.05462-11;
RA Antunes A., Alam I., Bajic V.B., Stingl U.;
RT "Genome sequence of Halorhabdus tiamatea, the first archaeon isolated from
RT a deep-sea anoxic brine lake.";
RL J. Bacteriol. 193:4553-4554(2011).
RN [2] {ECO:0000313|EMBL:ERJ06750.1, ECO:0000313|Proteomes:UP000003861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SARL4B {ECO:0000313|EMBL:ERJ06750.1,
RC ECO:0000313|Proteomes:UP000003861};
RX PubMed=24324765;
RA Alam I., Antunes A., Kamau A.A., Ba Alawi W., Kalkatawi M., Stingl U.,
RA Bajic V.B.;
RT "INDIGO - INtegrated Data Warehouse of MIcrobial GenOmes with Examples from
RT the Red Sea Extremophiles.";
RL PLoS ONE 8:E82210-E82210(2013).
RN [3] {ECO:0000313|EMBL:CCQ33673.1, ECO:0000313|Proteomes:UP000015381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SARL4B {ECO:0000313|Proteomes:UP000015381}, and Type strain:
RC SARL4B {ECO:0000313|EMBL:CCQ33673.1};
RX PubMed=24428220; DOI=10.1111/1462-2920.12393;
RA Werner J., Ferrer M., Michel G., Mann A.J., Huang S., Juarez S.,
RA Ciordia S., Albar J.P., Alcaide M., La Cono V., Yakimov M.M., Antunes A.,
RA Taborda M., Da Costa M.S., Amann R.I., Gloeckner F.O., Golyshina O.V.,
RA Golyshin P.N., Teeling H.;
RT "Halorhabdus tiamatea: proteogenomics and glycosidase activity measurements
RT identify the first cultivated euryarchaeon from a deep-sea anoxic brine
RT lake as potential polysaccharide degrader.";
RL Environ. Microbiol. 16:2525-2537(2014).
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; HF571520; CCQ33673.1; -; Genomic_DNA.
DR EMBL; AFNT02000010; ERJ06750.1; -; Genomic_DNA.
DR RefSeq; WP_008527712.1; NZ_AFNT02000010.1.
DR STRING; 1033806.HTIA_1546; -.
DR GeneID; 23799904; -.
DR KEGG; hti:HTIA_1546; -.
DR PATRIC; fig|1033806.12.peg.1534; -.
DR eggNOG; arCOG01434; Archaea.
DR HOGENOM; CLU_028142_0_0_2; -.
DR OrthoDB; 6371at2157; -.
DR UniPathway; UPA00050; UER00065.
DR Proteomes; UP000003861; Unassembled WGS sequence.
DR Proteomes; UP000015381; 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:ERJ06750.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRNR:PIRNR038945};
KW Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697,
KW ECO:0000256|PIRNR:PIRNR038945}.
FT DOMAIN 83..391
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT REGION 395..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 147
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR038945-1"
FT BINDING 251..255
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR038945-1"
FT BINDING 390
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR038945-1"
FT MOD_RES 121
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR038945-2"
SQ SEQUENCE 423 AA; 45189 MW; CFD6FAD860A9C0C6 CRC64;
MTHLEITQDE PAEATDGVWL TCIECGEHFP PFEGIRYTCD ECGGLLEVRY ADLPTFEDFG
DDESAFHGGV WRYSDALPFD EGVSLPEGNT PLHDVPRLED EIGVERLRVK HEGMNPTGSF
KDRGMTVGVR VAQEIGVDRL ACASTGNTSA ALSAYGSRAG LEVLVLLPAG KVAAGKIAQA
SLHGARILEV DGNFDRCLDI VKDLADRGEA YLLNSLNPFR LEGQKTIALE IMEQFRAEEG
QFPDRIVLPV GNAGNTAALY KAFRELETTG AIDENQIPKI TGVQAAGSAP LVEAIEEGWD
HIERWDDVET KATAIRIGNP VNAPKALPGV RETGGTAVAV SDEEITDAQR SLAEEGVGVE
PASAASIAGL RTLRAEGVVG DDEQVVCLTT GHLLKDPDAA AEAGTDPEPV PADTDDVLEH
LRS
//
