ID A0RPW0_CAMFF Unreviewed; 580 AA.
AC A0RPW0;
DT 09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=Threonine synthase {ECO:0000256|ARBA:ARBA00018679};
DE EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028};
GN OrderedLocusNames=CFF8240_1082 {ECO:0000313|EMBL:ABK82229.1};
OS Campylobacter fetus subsp. fetus (strain 82-40).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360106 {ECO:0000313|EMBL:ABK82229.1, ECO:0000313|Proteomes:UP000000760};
RN [1] {ECO:0000313|Proteomes:UP000000760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=82-40 {ECO:0000313|Proteomes:UP000000760};
RA Fouts D.E., Nelson K.E.;
RT "Sequence of Campylobacter fetus subsp. fetus 82-40.";
RL Submitted (NOV-2006) 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 5/5. {ECO:0000256|ARBA:ARBA00004979}.
CC -!- SIMILARITY: Belongs to the CutA family.
CC {ECO:0000256|ARBA:ARBA00010169}.
CC -!- SIMILARITY: Belongs to the threonine synthase family.
CC {ECO:0000256|ARBA:ARBA00005517}.
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DR EMBL; CP000487; ABK82229.1; -; Genomic_DNA.
DR AlphaFoldDB; A0RPW0; -.
DR KEGG; cff:CFF8240_1082; -.
DR eggNOG; COG0498; Bacteria.
DR eggNOG; COG1324; Bacteria.
DR HOGENOM; CLU_015170_3_1_7; -.
DR UniPathway; UPA00050; UER00065.
DR Proteomes; UP000000760; 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:0010038; P:response to metal ion; IEA:InterPro.
DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01560; Thr-synth_2; 1.
DR Gene3D; 3.30.70.120; -; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR Gene3D; 3.90.1380.10; Threonine synthase, N-terminal domain; 1.
DR InterPro; IPR004323; Ion_tolerance_CutA.
DR InterPro; IPR011322; N-reg_PII-like_a/b.
DR InterPro; IPR015867; N-reg_PII/ATP_PRibTrfase_C.
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; PTHR43515; THREONINE SYNTHASE-LIKE 1; 1.
DR PANTHER; PTHR43515:SF1; THREONINE SYNTHASE-LIKE 1; 1.
DR Pfam; PF03091; CutA1; 1.
DR Pfam; PF00291; PALP; 1.
DR Pfam; PF14821; Thr_synth_N; 1.
DR SUPFAM; SSF54913; GlnB-like; 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:UP000000760};
KW Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697}.
FT DOMAIN 115..179
FT /note="Threonine synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14821"
FT DOMAIN 193..497
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 213
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ SEQUENCE 580 AA; 65631 MW; 837B6804F995F05F CRC64;
MIVLSTTPDE KIANKLAKEL VDKKAAACVN CIKDLKSFYT WKNEVQNDSE VLMMIKGNYK
KIKDVILKNH PYETPEVIAI KPKKIEKSYK KWLEKSTKIS PMLVGTRLNN NEEVSCVSLS
EALLQPAAKH GGLYAPINLP ILDDNFFKKA SKLKYDEIAM MVIKKFKFDI DKDIFKKALK
RYAKFDKEAV EIKKLNKNLY INELWHGPTR AFKDMALQPF GVILKELAKQ NNKKYLIMCA
TSGDTGPATL NTFSDVQNIK VVCIYPKDGT SEVQRLQMVN QKGKNLKSIG IKGNFDDAQK
ALKALLNDKS FKNELSNLGL NLSAANSVNF GRILFQIIYH IYVCIKINSN KKPIDIVVPS
GNFGNTLGAY YAKKMGANIG KIKIASNANN ILTELFTTGI YNLQDKKLIQ TISPAMDILI
SSNVERLLFD KFGSIRTKEL MDSLKNSGFY KLAQEELEEL KADFEADFCS DEECENYIKN
VSSKGILIDP HTATCLKLVD NDKLSVITST AQWVKFTPSM VKAIKNKPTQ DELVDMKELA
KEFDVKIPKS ILELFSQKEL HKDVIEQDKI KSNIINWLKK
//
