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Database: UniProt
Entry: C7LPW5_DESBD
LinkDB: C7LPW5_DESBD
Original site: C7LPW5_DESBD 
ID   C7LPW5_DESBD            Unreviewed;       482 AA.
AC   C7LPW5;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-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=Dbac_3375 {ECO:0000313|EMBL:ACU91447.1};
OS   Desulfomicrobium baculatum (strain DSM 4028 / VKM B-1378 / X)
OS   (Desulfovibrio baculatus).
OC   Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC   Desulfomicrobiaceae; Desulfomicrobium.
OX   NCBI_TaxID=525897 {ECO:0000313|EMBL:ACU91447.1, ECO:0000313|Proteomes:UP000002216};
RN   [1] {ECO:0000313|EMBL:ACU91447.1, ECO:0000313|Proteomes:UP000002216}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4028 / VKM B-1378 / X {ECO:0000313|Proteomes:UP000002216};
RX   PubMed=21304634; DOI=10.4056/sigs.13134;
RA   Copeland A., Spring S., Goker M., Schneider S., Lapidus A., Del Rio T.G.,
RA   Tice H., Cheng J.F., Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S.,
RA   Ivanova N., Mavrommatis K., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.C., Meincke L.,
RA   Sims D., Brettin T., Detter J.C., Han C., Chain P., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Lucas S.;
RT   "Complete genome sequence of Desulfomicrobium baculatum type strain (X).";
RL   Stand. Genomic Sci. 1:29-37(2009).
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; CP001629; ACU91447.1; -; Genomic_DNA.
DR   RefSeq; WP_015775534.1; NC_013173.1.
DR   AlphaFoldDB; C7LPW5; -.
DR   STRING; 525897.Dbac_3375; -.
DR   KEGG; dba:Dbac_3375; -.
DR   eggNOG; COG0498; Bacteria.
DR   HOGENOM; CLU_028142_0_1_7; -.
DR   UniPathway; UPA00050; UER00065.
DR   Proteomes; UP000002216; 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; cd01563; Thr-synth_1; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
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; PTHR48078:SF6; ACT DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR48078; THREONINE DEHYDRATASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00291; PALP; 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:ACU91447.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR604450-51};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002216};
KW   Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697}.
FT   DOMAIN          96..407
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   MOD_RES         132
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ   SEQUENCE   482 AA;  53228 MW;  3E1A1285C767CABD CRC64;
     MREANVFPTY RGEMEYVCLG CQARYPIDEL HYTCPSCKGV FLLEDTRFPE LEKTPGSAWR
     DIFDLRAATK NPALRGIFRF YELMAPVVAE EHIVYLGEGN TPVTRSSTAL ERLVGQSMAF
     KNDGQNPSAS FKDRGMACAY SYLRHLVAKH GWDNVLTICA STGDTSAAAA LYAAYVGEPL
     TSVVLLPQGK VTAQQLSQPL GSGAKVLEIP GVFDDCMKVV EYLADHYRVA LLNSKNAWRI
     LGQESYAFEV AQWYDWDLRG KVIFVPIGNA GNITAIMSGF LKLLRLGIIE TLPRIIGVQS
     EHADPVFRYY DQDPGHRRFE AVKVRPSVAQ AAMIGNPVSF PRVAFLAEQY QKLGGAGSFA
     VVQVSEQRII ESMLLANRHG HIACTQGGEC LAGLFKAKEL GLMEEGELAV LDATAHALKF
     AGFQDMYFHD GFGPEFEITP DRKLANVPRL VIDQQDKERL SEDAFTVQAA QNVVGILGLD
     KK
//
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