ID U4UV35_9RHOB Unreviewed; 478 AA.
AC U4UV35;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Threonine synthase {ECO:0000256|ARBA:ARBA00018679};
DE EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028};
GN ORFNames=HIMB11_03153 {ECO:0000313|EMBL:ERL96408.1};
OS Rhodobacteraceae bacterium HIMB11.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1366046 {ECO:0000313|EMBL:ERL96408.1, ECO:0000313|Proteomes:UP000016848};
RN [1] {ECO:0000313|EMBL:ERL96408.1, ECO:0000313|Proteomes:UP000016848}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HIMB11 {ECO:0000313|EMBL:ERL96408.1,
RC ECO:0000313|Proteomes:UP000016848};
RA Durham B.P., DeLong E.F., Rappe M.S.;
RT "Draft genome sequence of marine alphaproteobacterial strain HIMB11, the
RT first cultivated representative of a unique lineage within the Roseobacter
RT clade possessing a remarkably small genome.";
RL Submitted (AUG-2013) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ERL96408.1}.
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DR EMBL; AVDB01000017; ERL96408.1; -; Genomic_DNA.
DR AlphaFoldDB; U4UV35; -.
DR STRING; 1366046.HIMB11_03153; -.
DR PATRIC; fig|1366046.3.peg.3174; -.
DR eggNOG; COG0498; Bacteria.
DR OrthoDB; 9763107at2; -.
DR UniPathway; UPA00050; UER00065.
DR Proteomes; UP000016848; 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 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};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR604450-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000016848};
KW Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697}.
FT DOMAIN 2..80
FT /note="Threonine synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14821"
FT DOMAIN 99..396
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 112
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ SEQUENCE 478 AA; 52418 MW; ED10979516A556F8 CRC64;
MRYISTRGKA ASLSFKEALL VGLASDGGLY VPEAWPKLSF GEMKSFQGKP YAQVAFAVMS
PFVGGEIDDI DLRRMIEEAY ATFHHPAVTP LVQMGPNDWL LELFHGPTLA FKDVAMQILA
RLMDHVLSER EERLTIVGAT SGDTGGAALE AFKTCDGIDT FFMFPNGKVS DFQRRQMTTI
GAENCHAIAI DGSFDDCQSI VKDMFRHQSF ASTVRLSAVN SINWGRVMAQ VVYYFSAATV
LGAPEQSVSF TVPTGNFGDI YAGFVAKQMG LPINRLVIAT NENDILARTL ATGDHRLGPV
KSTITPSMDI QISSNFERLL FDAAGRDHAL VRDLMTALRD SRRYRLPDKM LQFIRDSFDA
DAVSEVETQE EVARIWKETG YLADPHTAIA VKVARDHADP DVPMITLSTA HPAKFSNAVR
DATGEAARPP IWGDVPLGST ETVAHLASDR ARVEEYILQH ARLTQGSVRS FASEGVTS
//
