ID Q73L88_TREDE Unreviewed; 396 AA.
AC Q73L88;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=phosphoserine phosphatase {ECO:0000256|ARBA:ARBA00012640};
DE EC=3.1.3.3 {ECO:0000256|ARBA:ARBA00012640};
GN OrderedLocusNames=TDE_1977 {ECO:0000313|EMBL:AAS12491.1};
OS Treponema denticola (strain ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153
OS / KCTC 15104).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=243275 {ECO:0000313|EMBL:AAS12491.1, ECO:0000313|Proteomes:UP000008212};
RN [1] {ECO:0000313|EMBL:AAS12491.1, ECO:0000313|Proteomes:UP000008212}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104
RC {ECO:0000313|Proteomes:UP000008212};
RX PubMed=15064399; DOI=10.1073/pnas.0307639101;
RA Seshadri R., Myers G.S., Tettelin H., Eisen J.A., Heidelberg J.F.,
RA Dodson R.J., Davidsen T.M., DeBoy R.T., Fouts D.E., Haft D.H., Selengut J.,
RA Ren Q., Brinkac L.M., Madupu R., Kolonay J., Durkin S.A., Daugherty S.C.,
RA Shetty J., Shvartsbeyn A., Gebregeorgis E., Geer K., Tsegaye G., Malek J.,
RA Ayodeji B., Shatsman S., McLeod M.P., Smajs D., Howell J.K., Pal S.,
RA Amin A., Vashisth P., McNeill T.Z., Xiang Q., Sodergren E., Baca E.,
RA Weinstock G.M., Norris S.J., Fraser C.M., Paulsen I.T.;
RT "Comparison of the genome of the oral pathogen Treponema denticola with
RT other spirochete genomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:5646-5651(2004).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-D-serine = D-serine + phosphate;
CC Xref=Rhea:RHEA:24873, ChEBI:CHEBI:15377, ChEBI:CHEBI:35247,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58680; EC=3.1.3.3;
CC Evidence={ECO:0000256|ARBA:ARBA00001197};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-serine = L-serine + phosphate;
CC Xref=Rhea:RHEA:21208, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57524; EC=3.1.3.3;
CC Evidence={ECO:0000256|ARBA:ARBA00000860};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC 3-phospho-D-glycerate: step 3/3. {ECO:0000256|ARBA:ARBA00005135}.
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DR EMBL; AE017226; AAS12491.1; -; Genomic_DNA.
DR RefSeq; NP_972580.1; NC_002967.9.
DR AlphaFoldDB; Q73L88; -.
DR STRING; 243275.TDE_1977; -.
DR PaxDb; 243275-TDE_1977; -.
DR KEGG; tde:TDE_1977; -.
DR PATRIC; fig|243275.7.peg.1868; -.
DR eggNOG; COG0560; Bacteria.
DR HOGENOM; CLU_035114_0_0_12; -.
DR OrthoDB; 355730at2; -.
DR Proteomes; UP000008212; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1440.320; -; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR PANTHER; PTHR43344; PHOSPHOSERINE PHOSPHATASE; 1.
DR PANTHER; PTHR43344:SF2; PHOSPHOSERINE PHOSPHATASE; 1.
DR Pfam; PF12710; HAD; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023299};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008212};
KW Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299}.
SQ SEQUENCE 396 AA; 45048 MW; 6316837C98CF42F3 CRC64;
MQFIHNAIML NDDALILKTG NWEPQNKKRL EKLIREKAFN GNYAVFDWDF TSIFYDTQDN
LFVYQIENLC FNLNPEEFNQ TIRAGIPQDE ILPHTINLEG RALTAGELSD DLNERYEFLY
KNYLGFSGKM SLAEITLTEE FIDFRAKMLV LMRGAASLCG VDIGQSVSTG MTIEELSVLT
EKAIDQGLKD EIKTYRVRSS SVLKGRSGEV EGGYRKGLRV QEEMQDLFSA LRKNGIEVYI
CSASQEDNVR VFASNPKYGY RLDSKNVFGR RRLLDENKKL TVIDNTSIPA TRKEGKAEAI
KKVLAPKHQN KAPVLIAGDG DGDFYMMDAF KDEALILIFN RSPKKEAKIY PLLMSGIKER
ENPDARIIVQ HRNNQKGCFI SKAPEEEKPL DSLPEK
//
