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Database: UniProt
Entry: Q0BPV1_GRABC
LinkDB: Q0BPV1_GRABC
Original site: Q0BPV1_GRABC 
ID   Q0BPV1_GRABC            Unreviewed;       482 AA.
AC   Q0BPV1;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   RecName: Full=Threonine synthase {ECO:0000256|ARBA:ARBA00018679};
DE            EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028};
GN   OrderedLocusNames=GbCGDNIH1_2253 {ECO:0000313|EMBL:ABI63151.1};
OS   Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Granulibacter.
OX   NCBI_TaxID=391165 {ECO:0000313|EMBL:ABI63151.1, ECO:0000313|Proteomes:UP000001963};
RN   [1] {ECO:0000313|EMBL:ABI63151.1, ECO:0000313|Proteomes:UP000001963}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1260 / CGDNIH1 {ECO:0000313|Proteomes:UP000001963};
RX   PubMed=17827295; DOI=10.1128/JB.00793-07;
RA   Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E.,
RA   Kupko J.J.III., Barbian K.D., Babar A., Dorward D.W., Holland S.M.;
RT   "Genome sequence analysis of the emerging human pathogenic acetic acid
RT   bacterium Granulibacter bethesdensis.";
RL   J. Bacteriol. 189:8727-8736(2007).
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; CP000394; ABI63151.1; -; Genomic_DNA.
DR   RefSeq; WP_011632953.1; NC_008343.2.
DR   AlphaFoldDB; Q0BPV1; -.
DR   STRING; 391165.GbCGDNIH1_2253; -.
DR   KEGG; gbe:GbCGDNIH1_2253; -.
DR   eggNOG; COG0498; Bacteria.
DR   HOGENOM; CLU_015170_1_0_5; -.
DR   OrthoDB; 9763107at2; -.
DR   UniPathway; UPA00050; UER00065.
DR   Proteomes; UP000001963; 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:ABI63151.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR604450-51};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001963};
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          93..327
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   482 AA;  52529 MW;  39F32BC0A7347960 CRC64;
     MRYISTRGEA PIRDFSGVLL AGLAEDGGLY MPESWPQFSH DEWRAMRGLP YPDLAARIIQ
     PFVGDCIPAE TLLTLCRDAY AGFTHPAIVP LVQLDHDVYT QELFHGPTLA FKDMAMQLLG
     RLFDYVLSQS DRRITIVGAT SGDTGSAAIE AVRGRDRVDI VILHPEGRTS TVQRRQMTTA
     IAPNIGNVAV RGTFDDCQDL VKAMFADTPF RQEMSLSAVN SINWARIAAQ IPYYVYAALQ
     LGAPDRAVAF SVPTGNFGNV LAAYAAHRMG LPVGKLVVAS NRNDILYRFL SANDMSARPV
     EPSLSPSMDI QVSSNFERVL FELLDRDPAA TAATIRAFRE TGRMPVADAT WQKARTLFQG
     FRMDDTDTEA AIRALRQETG YLADPHSVIG IAAARSLRNA GSLSAAGPVI AMATAHPAKF
     PDAMERATGE RPALPPHLSD LYDREERFTV ADNNLADIEA LVRNIAHRNT SPASSPVTGV
     PA
//
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