ID U4KCK8_9VIBR Unreviewed; 427 AA.
AC U4KCK8;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
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:CCO56493.1};
GN ORFNames=VIBNI_A0290 {ECO:0000313|EMBL:CCO56493.1};
OS Vibrio nigripulchritudo.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=28173 {ECO:0000313|EMBL:CCO56493.1, ECO:0000313|Proteomes:UP000016895};
RN [1] {ECO:0000313|EMBL:CCO56493.1, ECO:0000313|Proteomes:UP000016895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SnF1 {ECO:0000313|Proteomes:UP000016895};
RX PubMed=23739050; DOI=10.1038/ismej.2013.90;
RA Goudenege D., Labreuche Y., Krin E., Ansquer D., Mangenot S., Calteau A.,
RA Medigue C., Mazel D., Polz M.F., Le Roux F.;
RT "Comparative genomics of pathogenic lineages of Vibrio nigripulchritudo
RT identifies virulence-associated traits.";
RL ISME J. 7:1985-1996(2013).
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; FO203526; CCO56493.1; -; Genomic_DNA.
DR RefSeq; WP_022549661.1; NC_022528.1.
DR AlphaFoldDB; U4KCK8; -.
DR STRING; 28173.VIBNI_A0290; -.
DR GeneID; 61873272; -.
DR KEGG; vni:VIBNI_A0290; -.
DR PATRIC; fig|1260221.3.peg.273; -.
DR eggNOG; COG0498; Bacteria.
DR OrthoDB; 9763107at2; -.
DR UniPathway; UPA00050; UER00065.
DR Proteomes; UP000016895; Chromosome 1.
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; 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; PF00291; PALP; 1.
DR Pfam; PF14821; Thr_synth_N; 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:CCO56493.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR604450-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000016895};
KW Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697}.
FT DOMAIN 8..78
FT /note="Threonine synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14821"
FT DOMAIN 85..367
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 105
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ SEQUENCE 427 AA; 46520 MW; 1067367200451407 CRC64;
MKLYNIKEND EQVSFGQAVR QGLGRNQGLF FPSELPKFED VDALLAEDFV TRSGKILSAF
IGEELSPEQV NQLVDAAFQF PAPIKQVKDG VYALELFHGP TLAFKDFGGR FMAQSLAAVS
DGGKITILTA TSGDTGAAVA HAFYGMENIN VVILYPKGKI SPMQEKLFCT LGKNIHTVAI
NADFDACQSL VKHAFDDAAL REEIGLNSAN SINISRLMAQ ICYYFEAAAQ MSKEERENLV
VSVPSGNFGN LTAGLLAKAL GLPIKRFVAA TNANDTVPRY LETGKWDPKP TVATTSNAMD
VSQPNNWPRI EELCQIKGWG LDTLGKGAVT DEQSAESVRD LNGLGYLCEP HGAIAYRVLD
EQLQEGETGL FLCTAHPAKF KEVVDEILET DIDVPGPLAK HAAMELLSEE LDNDFDALKA
VLRRVQK
//
