ID A9V4R9_MONBE Unreviewed; 968 AA.
AC A9V4R9;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=threonine synthase {ECO:0000256|ARBA:ARBA00013028};
DE EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028};
GN ORFNames=MONBRDRAFT_27254 {ECO:0000313|EMBL:EDQ87502.1};
OS Monosiga brevicollis (Choanoflagellate).
OC Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Monosiga.
OX NCBI_TaxID=81824 {ECO:0000313|EMBL:EDQ87502.1, ECO:0000313|Proteomes:UP000001357};
RN [1] {ECO:0000313|EMBL:EDQ87502.1, ECO:0000313|Proteomes:UP000001357}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MX1 / ATCC 50154 {ECO:0000313|Proteomes:UP000001357};
RX PubMed=18273011; DOI=10.1038/nature06617;
RG JGI Sequencing;
RA King N., Westbrook M.J., Young S.L., Kuo A., Abedin M., Chapman J.,
RA Fairclough S., Hellsten U., Isogai Y., Letunic I., Marr M., Pincus D.,
RA Putnam N., Rokas A., Wright K.J., Zuzow R., Dirks W., Good M.,
RA Goodstein D., Lemons D., Li W., Lyons J.B., Morris A., Nichols S.,
RA Richter D.J., Salamov A., Bork P., Lim W.A., Manning G., Miller W.T.,
RA McGinnis W., Shapiro H., Tjian R., Grigoriev I.V., Rokhsar D.;
RT "The genome of the choanoflagellate Monosiga brevicollis and the origin of
RT metazoans.";
RL Nature 451:783-788(2008).
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; CH991559; EDQ87502.1; -; Genomic_DNA.
DR RefSeq; XP_001747762.1; XM_001747710.1.
DR AlphaFoldDB; A9V4R9; -.
DR STRING; 81824.A9V4R9; -.
DR EnsemblProtists; EDQ87502; EDQ87502; MONBRDRAFT_27254.
DR GeneID; 5893041; -.
DR KEGG; mbr:MONBRDRAFT_27254; -.
DR eggNOG; KOG2616; Eukaryota.
DR InParanoid; A9V4R9; -.
DR OMA; CIYGNLQ; -.
DR UniPathway; UPA00050; UER00065.
DR Proteomes; UP000001357; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0004795; F:threonine synthase activity; IBA:GO_Central.
DR GO; GO:0009088; P:threonine biosynthetic process; IBA:GO_Central.
DR CDD; cd01560; Thr-synth_2; 1.
DR Gene3D; 3.30.230.10; -; 2.
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 InterPro; IPR013750; GHMP_kinase_C_dom.
DR InterPro; IPR036554; GHMP_kinase_C_sf.
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; 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; PF00291; PALP; 1.
DR Pfam; PF14821; Thr_synth_N; 1.
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; 2.
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:UP000001357};
KW Signal {ECO:0000256|SAM:SignalP};
KW Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..968
FT /note="threonine synthase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002742779"
FT DOMAIN 214..301
FT /note="GHMP kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08544"
FT DOMAIN 341..420
FT /note="Threonine synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14821"
FT DOMAIN 464..696
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 480
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ SEQUENCE 968 AA; 105265 MW; 056A606C2F5B8EB1 CRC64;
MAALCCAVLC CAVLCCAVLC CAVLCLHLHV KWNGWGIRSK ADSRLSIDDI GLRRRWIHHR
QHGRNSKVTV RVPATTANLG SGYDCLGMAV DIWNELTVEL ASAFSIHIEG EGADVLPRNG
ENLVEEMLQA AAEIEGHIDN LSPCIYGNLQ IGVNNGERWD TTGIPVPAGL QCVVLTPNVP
MSTHEARAML PDKISREDAI FNIGRAALLI NCILTRDYEA LRAATEDRLH QPVRGSAKVM
PALYPVIQAA LDAGAKGAFL SGAGSSIMAL TVGARGDVYA QSTLERRDRQ VADAMLAAAR
ANGVDGTVRI TRPTAVGAHV VAVTETITRP GLAAQGDCPS YVSTRGGPAS AVSFEEAVMA
GLAPDGGLYV PNQIPKVTEE TMRAWRRLSF PKLAVEVMGK FIGQNEIPAG TLEALVQRSY
ATFDSAHVTP LIEILTNKVV SLARVLIVSQ SLRAAMLSQF SEDGSVYLLE QFHGPTCAFK
DVALQFVGNL FEYFLSRRNA QSEKPKHITV LGATSGDTGS AAIFGLRGKA NVDVIILHPE
GRVAPIQEAQ MTTVLDDNVH NVAVKGTFDD CQAMVKECFN DPEFRQRHTL AAVNSINWAR
ILAQIVYYFY AYFRYLDLSE IEAAALPPVA FVTPTGNFGN ALAGFYASQM GLPVSRLVVA
TNRNDILYRY FAHGDYTSRP VEPSLAPAMD IVVPSNFERY VYWLLDGDSV RCKAVMDKVK
LTGRLDFGAD QARLLQRAQA FFGAARASDD DIQGIVATYK KQRSYALCPH SAAGLFAMEH
GGAGGGGGVC VCVCVCVCVC VCVCVNVCPD CLTAGSMRRF RDQLAGPFIC LATAHPAKFG
EGLEEARSMQ PHLPPQLDGL TTQPRRCHHL EHSLEDLKAF VHETMSRRHA ELAELELFYN
QNEFYSYCHS GSKKPDLSEQ KISTDRHYIS EIHYPDPLNS SHLIQSPAPP LKPDRPTQSV
IYITLCVS
//
