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Entry: A0A2K8KRI5_9GAMM
LinkDB: A0A2K8KRI5_9GAMM
Original site: A0A2K8KRI5_9GAMM 
ID   A0A2K8KRI5_9GAMM        Unreviewed;       465 AA.
AC   A0A2K8KRI5;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Threonine synthase {ECO:0000256|ARBA:ARBA00018679};
DE            EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028};
GN   ORFNames=REIFOR_02200 {ECO:0000313|EMBL:ATX77333.1};
OS   Reinekea forsetii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Saccharospirillaceae; Reinekea.
OX   NCBI_TaxID=1336806 {ECO:0000313|EMBL:ATX77333.1, ECO:0000313|Proteomes:UP000229757};
RN   [1] {ECO:0000313|EMBL:ATX77333.1, ECO:0000313|Proteomes:UP000229757}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hel1_31_D35 {ECO:0000313|EMBL:ATX77333.1,
RC   ECO:0000313|Proteomes:UP000229757};
RX   PubMed=28000419;
RA   Avci B., Hahnke R.L., Chafee M., Fischer T., Gruber-Vodicka H.,
RA   Tegetmeyer H.E., Harder J., Fuchs B.M., Amann R.I., Teeling H.;
RT   "Genomic and physiological analyses of 'Reinekea forsetii' reveal a
RT   versatile opportunistic lifestyle during spring algae blooms.";
RL   Environ. Microbiol. 19:1209-1221(2017).
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; CP011797; ATX77333.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K8KRI5; -.
DR   KEGG; rfo:REIFOR_02200; -.
DR   OrthoDB; 9763107at2; -.
DR   UniPathway; UPA00050; UER00065.
DR   Proteomes; UP000229757; 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:0000313|EMBL:ATX77333.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR604450-51};
KW   Reference proteome {ECO:0000313|Proteomes:UP000229757};
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..403
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   465 AA;  51370 MW;  ABB8EFA4ECB8B523 CRC64;
     MKYISTRGNA PELEFEDVLL AGLASDGGLY VPKDLPHYSL DTIRSWRGLS YSKLAFKIIQ
     PFVGGAIDDA ALQQMLDDTY DNFGHKAVAP LTQLDNNEYV LELFQGPTLA FKDFALQLLG
     RLLDHVLTKR NERAVIVGAT SGDTGSAAIE GCKHSEFVDI FIMHPHNRVS EVQRKQMTTV
     LSDNVYNIAV EGNFDDCQNM VKACFADQGF LRGERRLVAV NSINWARIMA QVVYYFYASL
     NLGGPDRSLS FSVPTGNFGD IFAGYLAKNM GLPIDQLIVA TNKNDILHRT ISQNRYEKHA
     LAHTLTPSMD IVVSSNFERL LFDIYGRDGQ LLADLMTRMN SEPVELDSAR MAKVRELFDS
     HAVDDPQTCA TIATVFAETG YLLDPHTAIG VVAARACRRH SDRPMVTLGT AHPVKFGEAI
     NKAGLATPAL PHHMADLLER EERCSLLPNS LAAVQAFVVK NVFDA
//
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