ID D1B2Q2_SULD5 Unreviewed; 498 AA.
AC D1B2Q2;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Threonine synthase {ECO:0000256|ARBA:ARBA00018679};
DE EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028};
GN OrderedLocusNames=Sdel_1352 {ECO:0000313|EMBL:ACZ12372.1};
OS Sulfurospirillum deleyianum (strain ATCC 51133 / DSM 6946 / 5175).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Sulfurospirillaceae; Sulfurospirillum.
OX NCBI_TaxID=525898 {ECO:0000313|EMBL:ACZ12372.1, ECO:0000313|Proteomes:UP000002222};
RN [1] {ECO:0000313|Proteomes:UP000002222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51133 / DSM 6946 / 5175
RC {ECO:0000313|Proteomes:UP000002222};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Ovchinnikova G., Munk A.C., Lu M., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.F.,
RA Hugenholtz P., Woyke T., Wu D., Aumann P., Schneider S., Lang E.,
RA Spring S., Klenk H.P., Eisen J.A.;
RT "The complete genome of Sulfurospirillum deleyianum DSM 6946.";
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACZ12372.1, ECO:0000313|Proteomes:UP000002222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51133 / DSM 6946 / 5175
RC {ECO:0000313|Proteomes:UP000002222};
RX PubMed=21304697; DOI=10.4056/sigs.671209;
RA Sikorski J., Lapidus A., Copeland A., Glavina Del Rio T., Nolan M.,
RA Lucas S., Chen F., Tice H., Cheng J.F., Saunders E., Bruce D., Goodwin L.,
RA Pitluck S., Ovchinnikova G., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Brettin T., Detter J.C., Han C., Rohde M., Lang E., Spring S., Goker M.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P.;
RT "Complete genome sequence of Sulfurospirillum deleyianum type strain
RT (5175).";
RL Stand. Genomic Sci. 2:149-157(2010).
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; CP001816; ACZ12372.1; -; Genomic_DNA.
DR AlphaFoldDB; D1B2Q2; -.
DR STRING; 525898.Sdel_1352; -.
DR KEGG; sdl:Sdel_1352; -.
DR eggNOG; COG0498; Bacteria.
DR HOGENOM; CLU_015170_3_1_7; -.
DR UniPathway; UPA00050; UER00065.
DR Proteomes; UP000002222; 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; PTHR43515; THREONINE SYNTHASE-LIKE 1; 1.
DR PANTHER; PTHR43515:SF1; THREONINE SYNTHASE-LIKE 1; 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:ACZ12372.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR604450-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000002222};
KW Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697}.
FT DOMAIN 2..78
FT /note="Threonine synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14821"
FT DOMAIN 87..409
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 114
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ SEQUENCE 498 AA; 55708 MW; FC8AADE24EE208F4 CRC64;
MFIETRGNDG IKPQKVPFSY AILHPSASFG GLYVPETLPK LDAHFFENAA KKSYKEITLD
ILNLFQIDIE KEVMQKAVAL YDAFDDAHEP TPLVQIEDDL FVNELYHGPT RAFKDMALQP
FGYILSHLAQ KLNEKYLILA ATSGDTGPAT LDTFANKPNI NVVCLYPDGG TSDVQRLQMT
TQTSTNVKVL GIHGNFDDAQ SALKTLLASS TFKEALEAKE IKLSAANSVN FGRIIFQIIY
HIYAYIALLK QEKIKNGHPF YTIIPSGNFG NALGAYYAKK MGLPIEKILI ASNINNILTD
LITTGVYDLR HRHLLQTTSP AMDILISSNV ERVLFDKFGA SRTKACMEAL KEEKIYTLNA
DELALLREDF EAVYCDDSFG KEQIHHYANK GYIMDPHTAT CLKAYQALKA KPLPCVLCST
AEWTKFAPTM MNALNQDTKK YSDKEALVGI EHSLHVKIPA SIHALFNQPV IHDKVVHKEA
IEAEIFEFLN LTCKKECK
//
