ID A0A099TWB4_9HELI Unreviewed; 499 AA.
AC A0A099TWB4;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Threonine synthase {ECO:0000256|ARBA:ARBA00018679};
DE EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028};
GN Name=thrC {ECO:0000313|EMBL:STQ86103.1};
GN ORFNames=LS73_005835 {ECO:0000313|EMBL:TLE00050.1}, NCTC12714_00894
GN {ECO:0000313|EMBL:STQ86103.1};
OS Helicobacter muridarum.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=216 {ECO:0000313|EMBL:STQ86103.1, ECO:0000313|Proteomes:UP000255139};
RN [1] {ECO:0000313|EMBL:TLE00050.1, ECO:0000313|Proteomes:UP000029922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST1 {ECO:0000313|EMBL:TLE00050.1,
RC ECO:0000313|Proteomes:UP000029922};
RX PubMed=25428971;
RA Sheh A., Shen Z., Fox J.G.;
RT "Draft genome sequences of eight enterohepatic helicobacter species
RT isolated from both laboratory and wild rodents.";
RL Genome Announc. 2:e01218-e01214(2014).
RN [2] {ECO:0000313|EMBL:STQ86103.1, ECO:0000313|Proteomes:UP000255139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12714 {ECO:0000313|EMBL:STQ86103.1,
RC ECO:0000313|Proteomes:UP000255139};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) 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 threonine synthase family.
CC {ECO:0000256|ARBA:ARBA00005517}.
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DR EMBL; UGJE01000002; STQ86103.1; -; Genomic_DNA.
DR EMBL; JRPD02000011; TLE00050.1; -; Genomic_DNA.
DR RefSeq; WP_034558353.1; NZ_UGJE01000002.1.
DR AlphaFoldDB; A0A099TWB4; -.
DR STRING; 216.LS73_06210; -.
DR OrthoDB; 9763107at2; -.
DR UniPathway; UPA00050; UER00065.
DR Proteomes; UP000029922; Unassembled WGS sequence.
DR Proteomes; UP000255139; Unassembled WGS sequence.
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 Gene3D; 3.40.50.1100; -; 2.
DR Gene3D; 3.90.1380.10; Threonine synthase, N-terminal domain; 1.
DR InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
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; 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 Lyase {ECO:0000313|EMBL:STQ86103.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR604450-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000255139};
KW Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697}.
FT DOMAIN 100..413
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 115
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ SEQUENCE 499 AA; 56160 MW; 6DEB4E3F89401626 CRC64;
MNYLAQTRSN DETYKTFSDA ILDPNAKLGG LYTFNNIKPF SDFTWLKKAS YVDICNKVFS
QLGIIDINSN NISSYIQIAL KSYDSFRHKE ICPLVNISPN LYCLELYHGP TFAFKDMALQ
PFSKLLDSLA SSQKQKYLIL SATSGDTGPA TLQGFADSTN IRAICIYPKG GTSEVQRLQM
TTQDAKNLKV FGIQGDFDMA QNSLKLLLRK QSFRENLTNM GYALSAANSV NIGRIAFQII
YYFVIARDLY LQGIQEFSII VPSGNFGNAL AGFFAKQLGL QITKLCIASN PNDILSEFFN
TGIYDLRNKI LKQSYSPAMD ILKSSNIERL LFALFGANRT RQCMESLDKD LIFSLTKEEL
KTLQTLFEAH SFDDSSCLIG IKKAFNQGYV IDPHTSNAYL FAKLRESSIN GQTQVILSTA
YFAKFAKTTL KALKGDSDRI KSIGDLEALK EIQKEIRNNI NPNFTLESNI TSLFNKSEIH
THTYHIEDLE QEILNFCKD
//
