THRH_PSEAE
ID THRH_PSEAE Reviewed; 205 AA.
AC Q9I2Y2;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Phosphoserine phosphatase ThrH;
DE Short=PSP;
DE Short=PSPase;
DE EC=3.1.3.3 {ECO:0000269|PubMed:14699121};
GN Name=thrH; OrderedLocusNames=PA1757;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP FUNCTION.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10220164; DOI=10.1099/13500872-145-4-845;
RA Patte J.C., Clepet C., Bally M., Borne F., Mejean V., Foglino M.;
RT "ThrH, a homoserine kinase isozyme with in vivo phosphoserine phosphatase
RT activity in Pseudomonas aeruginosa.";
RL Microbiology 145:845-853(1999).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.47 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND
RP PHOSPHATE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND ACTIVE SITE.
RC STRAIN=ATCC 17933;
RX PubMed=14699121; DOI=10.1074/jbc.m311393200;
RA Singh S.K., Yang K., Karthikeyan S., Huynh T., Zhang X., Phillips M.A.,
RA Zhang H.;
RT "The thrH gene product of Pseudomonas aeruginosa is a dual activity enzyme
RT with a novel phosphoserine:homoserine phosphotransferase activity.";
RL J. Biol. Chem. 279:13166-13173(2004).
CC -!- FUNCTION: Phosphoserine phosphatase that mediates dephosphorylation of
CC phosphoserine in the serine biosynthesis pathway. Also able to
CC dephosphorylate other substrates such as phospho-L(or D)-threonine,
CC with lower activity. Shows phosphoserine:homoserine phosphotransferase
CC activity by transferring the phosphoryl group to homoserine using
CC phosphoserine as the phosphoryl group donor.
CC {ECO:0000269|PubMed:10220164, ECO:0000269|PubMed:14699121}.
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:14699121};
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:14699121};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:14699121};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:14699121};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.207 mM for O-phospho-L-serine {ECO:0000269|PubMed:14699121};
CC Note=kcat is 13.4 min(-1) with O-phospho-L-serine as substrate.;
CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC 3-phospho-D-glycerate: step 3/3.
CC -!- SIMILARITY: Belongs to the thrH family. {ECO:0000305}.
CC -!- CAUTION: Its ability to complement a strain lacking the homoserine
CC kinase thrB gene suggested that it acts as a homoserine kinase
CC (PubMed:10220164). The ability to rescue a thrB mutant is explained by
CC the phosphoserine:homoserine phosphotransferase activity in presence of
CC phosphoserine, in a mechanism different from homoserine kinase,
CC suggesting it is inappropriate to define it as a homoserine kinase
CC (PubMed:14699121). {ECO:0000305|PubMed:10220164,
CC ECO:0000305|PubMed:14699121}.
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DR EMBL; AE004091; AAG05146.1; -; Genomic_DNA.
DR PIR; A83427; A83427.
DR RefSeq; NP_250448.1; NC_002516.2.
DR RefSeq; WP_003098078.1; NZ_QZGE01000003.1.
DR PDB; 1RKU; X-ray; 1.47 A; A/B=1-205.
DR PDB; 1RKV; X-ray; 1.90 A; A/B=1-205.
DR PDBsum; 1RKU; -.
DR PDBsum; 1RKV; -.
DR AlphaFoldDB; Q9I2Y2; -.
DR SMR; Q9I2Y2; -.
DR STRING; 287.DR97_129; -.
DR PaxDb; Q9I2Y2; -.
DR PRIDE; Q9I2Y2; -.
DR EnsemblBacteria; AAG05146; AAG05146; PA1757.
DR GeneID; 877969; -.
DR KEGG; pae:PA1757; -.
DR PATRIC; fig|208964.12.peg.1820; -.
DR PseudoCAP; PA1757; -.
DR HOGENOM; CLU_097498_0_0_6; -.
DR InParanoid; Q9I2Y2; -.
DR OMA; YNDTAML; -.
DR PhylomeDB; Q9I2Y2; -.
DR BioCyc; PAER208964:G1FZ6-1788-MON; -.
DR UniPathway; UPA00135; UER00198.
DR EvolutionaryTrace; Q9I2Y2; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0046820; F:4-amino-4-deoxychorismate synthase activity; ISS:PseudoCAP.
DR GO; GO:0036424; F:L-phosphoserine phosphatase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0043899; F:phosphoserine:homoserine phosphotransferase activity; IDA:PseudoCAP.
DR GO; GO:0016311; P:dephosphorylation; IDA:UniProtKB.
DR GO; GO:0006564; P:L-serine biosynthetic process; IBA:GO_Central.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; ISS:PseudoCAP.
DR GO; GO:0009088; P:threonine biosynthetic process; IMP:PseudoCAP.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR011863; HSK-PSP.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR02137; HSK-PSP; 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..205
FT /note="Phosphoserine phosphatase ThrH"
FT /id="PRO_0000429057"
FT ACT_SITE 7
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:14699121"
FT ACT_SITE 9
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:14699121"
FT BINDING 7
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:14699121"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:14699121"
FT BINDING 15
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 46
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 90..91
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 133
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 152
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:14699121"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:1RKU"
FT TURN 10..12
FT /evidence="ECO:0007829|PDB:1RKU"
FT HELIX 16..24
FT /evidence="ECO:0007829|PDB:1RKU"
FT HELIX 27..30
FT /evidence="ECO:0007829|PDB:1RKU"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:1RKU"
FT HELIX 39..52
FT /evidence="ECO:0007829|PDB:1RKU"
FT HELIX 57..64
FT /evidence="ECO:0007829|PDB:1RKU"
FT HELIX 73..81
FT /evidence="ECO:0007829|PDB:1RKU"
FT STRAND 84..93
FT /evidence="ECO:0007829|PDB:1RKU"
FT HELIX 94..103
FT /evidence="ECO:0007829|PDB:1RKU"
FT STRAND 109..116
FT /evidence="ECO:0007829|PDB:1RKU"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:1RKU"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:1RKU"
FT HELIX 132..142
FT /evidence="ECO:0007829|PDB:1RKU"
FT STRAND 146..151
FT /evidence="ECO:0007829|PDB:1RKU"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:1RKV"
FT HELIX 157..162
FT /evidence="ECO:0007829|PDB:1RKU"
FT STRAND 163..170
FT /evidence="ECO:0007829|PDB:1RKU"
FT HELIX 173..178
FT /evidence="ECO:0007829|PDB:1RKU"
FT HELIX 188..198
FT /evidence="ECO:0007829|PDB:1RKU"
SQ SEQUENCE 205 AA; 23533 MW; F33CE8FCC4C63B62 CRC64;
MEIACLDLEG VLVPEIWIAF AEKTGIDALK ATTRDIPDYD VLMKQRLRIL DEHGLKLGDI
QEVIATLKPL EGAVEFVDWL RERFQVVILS DTFYEFSQPL MRQLGFPTLL CHKLEIDDSD
RVVGYQLRQK DPKRQSVIAF KSLYYRVIAA GDSYNDTTML SEAHAGILFH APENVIREFP
QFPAVHTYED LKREFLKASS RSLSL
