ID C6XC49_METGS Unreviewed; 477 AA.
AC C6XC49;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Threonine synthase {ECO:0000256|ARBA:ARBA00018679};
DE EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028};
GN OrderedLocusNames=Msip34_0876 {ECO:0000313|EMBL:ACT50124.1};
OS Methylovorus glucosotrophus (strain SIP3-4).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Methylophilaceae; Methylovorus.
OX NCBI_TaxID=582744 {ECO:0000313|EMBL:ACT50124.1, ECO:0000313|Proteomes:UP000002743};
RN [1] {ECO:0000313|Proteomes:UP000002743}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SIP3-4 {ECO:0000313|Proteomes:UP000002743};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Clum A., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Kayluzhnaya M., Chistoserdova L.;
RT "Complete sequence of chromosome of Methylovorus sp. SIP3-4.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACT50124.1, ECO:0000313|Proteomes:UP000002743}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SIP3-4 {ECO:0000313|EMBL:ACT50124.1,
RC ECO:0000313|Proteomes:UP000002743};
RX PubMed=21622745; DOI=10.1128/JB.00404-11;
RA Lapidus A., Clum A., Labutti K., Kaluzhnaya M.G., Lim S., Beck D.A.,
RA Glavina Del Rio T., Nolan M., Mavromatis K., Huntemann M., Lucas S.,
RA Lidstrom M.E., Ivanova N., Chistoserdova L.;
RT "Genomes of three methylotrophs from a single niche uncover genetic and
RT metabolic divergence of Methylophilaceae.";
RL J. Bacteriol. 193:3757-3764(2011).
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; CP001674; ACT50124.1; -; Genomic_DNA.
DR RefSeq; WP_015829679.1; NC_012969.1.
DR AlphaFoldDB; C6XC49; -.
DR STRING; 582744.Msip34_0876; -.
DR KEGG; mei:Msip34_0876; -.
DR eggNOG; COG0498; Bacteria.
DR HOGENOM; CLU_015170_1_0_4; -.
DR OrthoDB; 9763107at2; -.
DR UniPathway; UPA00050; UER00065.
DR Proteomes; UP000002743; 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:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01560; Thr-synth_2; 1.
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; PTHR42690; THREONINE SYNTHASE FAMILY MEMBER; 1.
DR PANTHER; PTHR42690:SF1; THREONINE SYNTHASE-LIKE 2; 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:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:ACT50124.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR604450-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000002743};
KW Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697}.
FT DOMAIN 2..79
FT /note="Threonine synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14821"
FT DOMAIN 102..338
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 120
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ SEQUENCE 477 AA; 52325 MW; 35FE46B03B9C7FF8 CRC64;
MKYISTRGQS PALSFTEILL GGLAPDGGLY LPEQYPQLSD ADLTRLRGMN YRDLAFSILS
LLADDIPPAD LRAIVDKTYR ADVYAYARPE QNAEDITPTL KLEDNLYLLS LSNGPTLAFK
DMAMQLLGNL FEYVLAKKGE TTNILGATSG DTGSAAEYAM RGKKGVKVFM LSPHKKMSRF
QTAQMFSLQD ENIFNIAVNG VFDDAQDIVK AVSNDAAFKA RNKIGAVNSI NWARVAAQVV
YYFKGYFAVT RSNTEKVSFA VPSGNFGNVC AGHVARMMGL PIDKLVVATN ENDVLDEFFK
TGVYRPRGSA NTYHTSSPSM DISKASNFER FVFDLTGRDA AKVRALWSKV DQGGAFDLNE
DGLFAQVADY GFVSGSSNHA ARMQTIRETQ AKYGVTIDTH TADGLKVALQ VREPAIPMLV
LETALPVKFE DAIQEALGHK PERPASLQGL EDLPQRFEVM DADVQAIKQF IVDHTAD
//
