ID A0A0G3H195_9CORY Unreviewed; 495 AA.
AC A0A0G3H195;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
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:AKK06555.1};
GN ORFNames=CMUST_11200 {ECO:0000313|EMBL:AKK06555.1};
OS Corynebacterium mustelae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=571915 {ECO:0000313|EMBL:AKK06555.1, ECO:0000313|Proteomes:UP000035199};
RN [1] {ECO:0000313|EMBL:AKK06555.1, ECO:0000313|Proteomes:UP000035199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45274 {ECO:0000313|EMBL:AKK06555.1,
RC ECO:0000313|Proteomes:UP000035199};
RX PubMed=26358597;
RA Ruckert C., Eimer J., Winkler A., Tauch A.;
RT "Complete Genome Sequence of the Type Strain Corynebacterium mustelae DSM
RT 45274, Isolated from Various Tissues of a Male Ferret with Lethal Sepsis.";
RL Genome Announc. 3:e01012-15(2015).
RN [2] {ECO:0000313|Proteomes:UP000035199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45274 {ECO:0000313|Proteomes:UP000035199};
RA Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT "Complete genome sequence of Corynebacterium mustelae DSM 45274, isolated
RT from various tissues of a male ferret with lethal sepsis.";
RL Submitted (MAY-2015) 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; CP011542; AKK06555.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G3H195; -.
DR STRING; 571915.CMUST_11200; -.
DR KEGG; cmv:CMUST_11200; -.
DR PATRIC; fig|571915.4.peg.2393; -.
DR UniPathway; UPA00050; UER00065.
DR Proteomes; UP000035199; 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:AKK06555.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR604450-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000035199};
KW Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697}.
FT DOMAIN 22..104
FT /note="Threonine synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14821"
FT DOMAIN 105..356
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 138
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ SEQUENCE 495 AA; 54810 MW; A7C2C8EB4CD6C94E CRC64;
MNYLPPVKPW FEPEHANLVS VHYISTRDKN KTPATFSDIL LGGLAPDGGL YLPEEYPQLT
LEVLSNWREL LKTQGYHALA AEVLKLFIDD IPEADIEAIC ARAYRTPTFS TEEIVPVTKL
QDGIYIGHLS EGPTAAFKDM AMQLLGELFE YELNRRGETL NILGATSGDT GSAAEYAMRG
RTGIKVFMLT PKGRMTAFQQ AQMFGLADEN IFNIALDGVF DDCQDVVKAV SADTVFKVNN
RIGAVNSINW ARLMAQVVYY ISSWLKVTDA DDQKVSFCVP TGNFGDICAG HIAKQMGLPI
DRLIVATNEN DVLDEFFRTG EYRVRSAADT LETSSPSMDI SRASNFERFI FDLLGRDAER
ISDLFGSQVP TGGFSLVGDP AFGIIPTRYG FLSGRSTHAD RVAVIKDCFD NYGVLIDPHT
ADGVKVAREW LDQVDSPIVC LETALPVKFA ETITEATGFF PPIPERFAHV MDAERHVTDL
PNDVNTVKEF ITERL
//