ID F2UH39_SALR5 Unreviewed; 882 AA.
AC F2UH39;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Threonine synthase {ECO:0000313|EMBL:EGD76438.1};
GN ORFNames=PTSG_12606 {ECO:0000313|EMBL:EGD76438.1};
OS Salpingoeca rosetta (strain ATCC 50818 / BSB-021).
OC Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Salpingoeca.
OX NCBI_TaxID=946362 {ECO:0000313|Proteomes:UP000007799};
RN [1] {ECO:0000313|Proteomes:UP000007799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50818 {ECO:0000313|Proteomes:UP000007799};
RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "Annotation of Salpingoeca rosetta.";
RL Submitted (AUG-2009) 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=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 4/5. {ECO:0000256|ARBA:ARBA00005015}.
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 GHMP kinase family. Homoserine kinase
CC subfamily. {ECO:0000256|ARBA:ARBA00007370}.
CC -!- SIMILARITY: Belongs to the threonine synthase family.
CC {ECO:0000256|ARBA:ARBA00005517}.
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DR EMBL; GL832974; EGD76438.1; -; Genomic_DNA.
DR RefSeq; XP_004991353.1; XM_004991296.1.
DR AlphaFoldDB; F2UH39; -.
DR STRING; 946362.F2UH39; -.
DR EnsemblProtists; EGD76438; EGD76438; PTSG_12606.
DR GeneID; 16071915; -.
DR KEGG; sre:PTSG_12606; -.
DR eggNOG; KOG1537; Eukaryota.
DR eggNOG; KOG2616; Eukaryota.
DR InParanoid; F2UH39; -.
DR OMA; CIYGNLQ; -.
DR OrthoDB; 275600at2759; -.
DR UniPathway; UPA00050; UER00064.
DR Proteomes; UP000007799; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004413; F:homoserine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0004795; F:threonine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01560; Thr-synth_2; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR Gene3D; 3.30.70.890; GHMP kinase, C-terminal domain; 1.
DR Gene3D; 3.90.1380.10; Threonine synthase, N-terminal domain; 1.
DR HAMAP; MF_00384; Homoser_kinase; 1.
DR InterPro; IPR013750; GHMP_kinase_C_dom.
DR InterPro; IPR036554; GHMP_kinase_C_sf.
DR InterPro; IPR006204; GHMP_kinase_N_dom.
DR InterPro; IPR006203; GHMP_knse_ATP-bd_CS.
DR InterPro; IPR000870; Homoserine_kinase.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
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; TIGR00191; thrB; 1.
DR NCBIfam; TIGR00260; thrC; 1.
DR PANTHER; PTHR42690; THREONINE SYNTHASE FAMILY MEMBER; 1.
DR PANTHER; PTHR42690:SF1; THREONINE SYNTHASE-LIKE 2; 1.
DR Pfam; PF08544; GHMP_kinases_C; 1.
DR Pfam; PF00288; GHMP_kinases_N; 1.
DR Pfam; PF00291; PALP; 1.
DR Pfam; PF14821; Thr_synth_N; 1.
DR PRINTS; PR00958; HOMSERKINASE.
DR SUPFAM; SSF55060; GHMP Kinase, C-terminal domain; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
DR PROSITE; PS00627; GHMP_KINASES_ATP; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR604450-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000007799};
KW Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 86..147
FT /note="GHMP kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00288"
FT DOMAIN 210..287
FT /note="GHMP kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08544"
FT DOMAIN 339..420
FT /note="Threonine synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14821"
FT DOMAIN 428..689
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 460
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ SEQUENCE 882 AA; 96057 MW; 7496C16A701AA707 CRC64;
MSHTVRSGVT VRVPATTANM GPGYDSLGMA LDLWNELTVE YASMFSIHIQ GEGADVLPRN
EDNFVVKGVQ LAFERAGKPM PTLAFFCKNE IPFGSGLGSS SAGIISGILA GLVLSGQQVK
VKDGEELLQM AASIEGHVDN IAPCIYGNLQ IGFHTGERWQ TQEIAVPSSL QCVVLTPNTP
MNTKEARAML KSEVPRDDAI FNIARTALLV RAFQTGDLDS LRHATEDKLH QPVRGSDKVL
PALFPVIKAA LDAGAKGAFL SGAGSSILAI TTGARGEVAV QDASERFDAA VAAAMTAAAE
ACGVQGRITI TRPTPLGAHV VAIRETIAPS LSFKSTGPRY VSTRRSDENA SVSFEEAVMH
GLAHDGGLYV PREVPTVSID MLKEWSTLSF PDLAAAVMRL YIGVDEISDA ALSELVHRSY
SRFTSSHVTP LVKLTPGTTA EHAPPTYVLE QFHGPTCAFK DVALQFVGNL FEFFLARKNQ
HLPEEDRHAI TVLGATSGDT GSAAIEGLRG KENVEVFILH PHKRVAPIQE AQMTTILDAN
VHNVAVDGAF DDCQSMVKTL FQDEEFREKH HLAAVNSINW ARILAQIVYY FYMYFRWVEQ
EHTAIGTTLN VVVPTGNFGN ILAGFYAKRM GLPLGKLVVA TNRNDILYRF LRHRDYTARP
VEPSLAPAMD IVVPSNFERF LYFLMDNNPH KTKALMKRIK SSGTLDLGKN KDELYKIVDS
FFDAGRASDE DIKAAIWRYR KLYNYLPCPH TATALHTMQL VRGDGEDLAG VPASHFVCLA
TAHPGKFRET DAPTDVPPPL PPQLKGLHLK PKRCAHIGND LTELKDFMDT TLAEREQAKD
VAGTSSCMWC AQMCCGRWDL VAAAGVGAAV AIASLHLLNR RT
//