SERB_VIBCH
ID SERB_VIBCH Reviewed; 328 AA.
AC Q9KPM2;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Phosphoserine phosphatase {ECO:0000305|PubMed:25848029};
DE Short=PSP {ECO:0000250|UniProtKB:Q58989};
DE Short=PSPase {ECO:0000250|UniProtKB:Q58989};
DE EC=3.1.3.3 {ECO:0000269|PubMed:25848029};
DE AltName: Full=O-phosphoserine phosphohydrolase {ECO:0000250|UniProtKB:Q58989};
GN OrderedLocusNames=VC_2345 {ECO:0000312|EMBL:AAF95488.1};
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277 {ECO:0000312|Proteomes:UP000000584};
RN [1] {ECO:0000312|Proteomes:UP000000584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961
RC {ECO:0000312|Proteomes:UP000000584};
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
RN [2] {ECO:0000305}
RP CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=25848029; DOI=10.1073/pnas.1423570112;
RA Huang H., Pandya C., Liu C., Al-Obaidi N.F., Wang M., Zheng L.,
RA Toews Keating S., Aono M., Love J.D., Evans B., Seidel R.D.,
RA Hillerich B.S., Garforth S.J., Almo S.C., Mariano P.S., Dunaway-Mariano D.,
RA Allen K.N., Farelli J.D.;
RT "Panoramic view of a superfamily of phosphatases through substrate
RT profiling.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:E1974-E1983(2015).
RN [3] {ECO:0007744|PDB:3N28}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 4-327.
RA Patskovsky Y., Ramagopal U., Toro R., Rutter M., Miller S., Sauder J.M.,
RA Burley S.K., Almo S.C.;
RT "Crystal structure of phosphoserine phosphatase from Vibrio cholerae.";
RL Submitted (MAY-2010) to the PDB data bank.
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:0000269|PubMed:25848029};
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:0000269|PubMed:25848029};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:25848029};
CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC 3-phospho-D-glycerate: step 3/3. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. SerB family.
CC {ECO:0000305}.
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DR EMBL; AE003852; AAF95488.1; -; Genomic_DNA.
DR PIR; A82087; A82087.
DR RefSeq; NP_231975.1; NC_002505.1.
DR PDB; 3N28; X-ray; 2.30 A; A=4-327.
DR PDBsum; 3N28; -.
DR AlphaFoldDB; Q9KPM2; -.
DR SMR; Q9KPM2; -.
DR STRING; 243277.VC_2345; -.
DR DNASU; 2613141; -.
DR EnsemblBacteria; AAF95488; AAF95488; VC_2345.
DR KEGG; vch:VC_2345; -.
DR PATRIC; fig|243277.26.peg.2232; -.
DR eggNOG; COG0560; Bacteria.
DR HOGENOM; CLU_036368_4_0_6; -.
DR OMA; CINEPDL; -.
DR BioCyc; VCHO:VC2345-MON; -.
DR UniPathway; UPA00135; UER00198.
DR EvolutionaryTrace; Q9KPM2; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0036424; F:L-phosphoserine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR GO; GO:0016311; P:dephosphorylation; IBA:GO_Central.
DR GO; GO:0006564; P:L-serine biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR004469; PSP.
DR InterPro; IPR041449; SerB_N.
DR Pfam; PF18429; DUF5609; 1.
DR SFLD; SFLDF00029; phosphoserine_phosphatase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR00338; serB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Hydrolase; Magnesium; Metal-binding;
KW Reference proteome; Serine biosynthesis.
FT CHAIN 1..328
FT /note="Phosphoserine phosphatase"
FT /evidence="ECO:0000305"
FT /id="PRO_0000435470"
FT ACT_SITE 113
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT ACT_SITE 115
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 113
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 115
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 201..202
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 246
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 269
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 272
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:3N28"
FT HELIX 15..18
FT /evidence="ECO:0007829|PDB:3N28"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:3N28"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:3N28"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:3N28"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:3N28"
FT HELIX 46..56
FT /evidence="ECO:0007829|PDB:3N28"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:3N28"
FT STRAND 71..78
FT /evidence="ECO:0007829|PDB:3N28"
FT HELIX 82..91
FT /evidence="ECO:0007829|PDB:3N28"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:3N28"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:3N28"
FT HELIX 117..131
FT /evidence="ECO:0007829|PDB:3N28"
FT HELIX 134..145
FT /evidence="ECO:0007829|PDB:3N28"
FT HELIX 151..160
FT /evidence="ECO:0007829|PDB:3N28"
FT TURN 161..164
FT /evidence="ECO:0007829|PDB:3N28"
FT HELIX 169..174
FT /evidence="ECO:0007829|PDB:3N28"
FT HELIX 183..192
FT /evidence="ECO:0007829|PDB:3N28"
FT STRAND 196..204
FT /evidence="ECO:0007829|PDB:3N28"
FT HELIX 205..215
FT /evidence="ECO:0007829|PDB:3N28"
FT STRAND 218..228
FT /evidence="ECO:0007829|PDB:3N28"
FT STRAND 231..238
FT /evidence="ECO:0007829|PDB:3N28"
FT HELIX 243..257
FT /evidence="ECO:0007829|PDB:3N28"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:3N28"
FT STRAND 264..268
FT /evidence="ECO:0007829|PDB:3N28"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:3N28"
FT HELIX 274..279
FT /evidence="ECO:0007829|PDB:3N28"
FT STRAND 280..287
FT /evidence="ECO:0007829|PDB:3N28"
FT HELIX 290..293
FT /evidence="ECO:0007829|PDB:3N28"
FT STRAND 296..303
FT /evidence="ECO:0007829|PDB:3N28"
FT HELIX 306..318
FT /evidence="ECO:0007829|PDB:3N28"
SQ SEQUENCE 328 AA; 36116 MW; 7B174A8EE20D7011 CRC64;
MDMDALTTLP IKKHTALLNR FPETRFVTQL AKKRASWIVF GHYLTPAQFE DMDFFTNRFN
AILDMWKVGR YEVALMDGEL TSEHETILKA LELDYARIQD VPDLTKPGLI VLDMDSTAIQ
IECIDEIAKL AGVGEEVAEV TERAMQGELD FEQSLRLRVS KLKDAPEQIL SQVRETLPLM
PELPELVATL HAFGWKVAIA SGGFTYFSDY LKEQLSLDYA QSNTLEIVSG KLTGQVLGEV
VSAQTKADIL LTLAQQYDVE IHNTVAVGDG ANDLVMMAAA GLGVAYHAKP KVEAKAQTAV
RFAGLGGVVC ILSAALVAQQ KLSWKSKP
