ID A0A1S2XBR1_CICAR Unreviewed; 531 AA.
AC A0A1S2XBR1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, 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 Name=LOC101492251 {ECO:0000313|RefSeq:XP_004486860.1};
OS Cicer arietinum (Chickpea) (Garbanzo).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Cicereae; Cicer.
OX NCBI_TaxID=3827 {ECO:0000313|Proteomes:UP000087171, ECO:0000313|RefSeq:XP_004486860.1};
RN [1] {ECO:0000313|RefSeq:XP_004486860.1}
RP IDENTIFICATION.
RC TISSUE=Etiolated seedlings {ECO:0000313|RefSeq:XP_004486860.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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|ARBA:ARBA00003648}.
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 RefSeq; XP_004486860.1; XM_004486803.3.
DR AlphaFoldDB; A0A1S2XBR1; -.
DR STRING; 3827.A0A1S2XBR1; -.
DR PaxDb; 3827-XP_004486860-1; -.
DR GeneID; 101492251; -.
DR KEGG; cam:101492251; -.
DR eggNOG; ENOG502QSQC; Eukaryota.
DR OrthoDB; 544888at2759; -.
DR UniPathway; UPA00050; UER00065.
DR Proteomes; UP000087171; Chromosome Ca1.
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; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR NCBIfam; TIGR00260; thrC; 1.
DR PANTHER; PTHR10314; CYSTATHIONINE BETA-SYNTHASE; 1.
DR PANTHER; PTHR10314:SF248; THREONINE SYNTHASE 1, CHLOROPLASTIC; 1.
DR Pfam; PF00291; PALP; 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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR604450-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000087171};
KW Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697}.
FT DOMAIN 169..476
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 30..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 207
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ SEQUENCE 531 AA; 58649 MW; 69A06C603A28665F CRC64;
MASSTLFQSS PFSLNTNTKP YSLPISTKPI HFTVKSQSQS QPQPLTQNNT PTPSPSPSSK
LRRPADENIR DEARRKNVSQ HLFSAKYVPF NADPSSTESY SLDEIVYRSQ SGDLLDVQHD
LTALKKFDGA YWRNLFDSRV GKTTWPYGSG VWSKKEWVLP EIDDDDIVSA FEGNSNLFWA
ERFGKQFLGM NELWVKHCGI SHTGSFKDLG MTVLVSQVNR LRKMNRPVVG VGCASTGDTS
AALSAYCASA GIPSIVFLPA NRISIAQLVQ PIANGAFVLS IDTDFDGCMQ LIREVTAELP
IYLANSLNSL RLEGQKTAAI EILQQFDWQV PDWVIVPGGN LGNIYAFYKG FQMCKELGLV
DRIPRLVCAQ AANANPLYLY FKSGWKEFKP VRAQTTFASA IQIGDPVSID RAVHALRSCN
GIVEEATEEE LMDAMAQADS TGMFTCPHTG VALTALFKLR NSGVIKPTDR TVVVSTAHGL
KFTQSKIEYH SKGIKDLACQ FANPPMQVKA DFGSVMDVLS KYLQSKAPRY H
//
