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Database: UniProt
Entry: A0A397TPR0_9GLOM
LinkDB: A0A397TPR0_9GLOM
Original site: A0A397TPR0_9GLOM 
ID   A0A397TPR0_9GLOM        Unreviewed;       610 AA.
AC   A0A397TPR0;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=phosphoserine phosphatase {ECO:0000256|ARBA:ARBA00012640};
DE            EC=3.1.3.3 {ECO:0000256|ARBA:ARBA00012640};
DE   AltName: Full=O-phosphoserine phosphohydrolase {ECO:0000256|ARBA:ARBA00031693};
GN   ORFNames=C1645_814685 {ECO:0000313|EMBL:RIA97021.1};
OS   Glomus cerebriforme.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC   Glomeromycetes; Glomerales; Glomeraceae; Glomus.
OX   NCBI_TaxID=658196 {ECO:0000313|EMBL:RIA97021.1, ECO:0000313|Proteomes:UP000265703};
RN   [1] {ECO:0000313|EMBL:RIA97021.1, ECO:0000313|Proteomes:UP000265703}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DAOM 227022 {ECO:0000313|EMBL:RIA97021.1,
RC   ECO:0000313|Proteomes:UP000265703};
RA   Morin E., San Clemente H., Chen E.C.H., De La Providencia I., Hainaut M.,
RA   Kuo A., Kohler A., Murat C., Tang N., Roy S., Loubradou J., Henrissat B.,
RA   Grigoriev I.V., Corradi N., Roux C., Martin F.M.;
RT   "Comparative genomics reveals the genomic features of Rhizophagus
RT   irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their
RT   symbiotic lifestyle signature.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. SerB family.
CC       {ECO:0000256|ARBA:ARBA00009184}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RIA97021.1}.
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DR   EMBL; QKYT01000036; RIA97021.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A397TPR0; -.
DR   STRING; 658196.A0A397TPR0; -.
DR   UniPathway; UPA00135; UER00198.
DR   Proteomes; UP000265703; Unassembled WGS sequence.
DR   GO; GO:0036424; F:L-phosphoserine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd07500; HAD_PSP; 1.
DR   CDD; cd14447; SPX; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR004469; PSP.
DR   InterPro; IPR004331; SPX_dom.
DR   NCBIfam; TIGR01488; HAD-SF-IB; 1.
DR   NCBIfam; TIGR00338; serB; 1.
DR   PANTHER; PTHR43344; PHOSPHOSERINE PHOSPHATASE; 1.
DR   PANTHER; PTHR43344:SF2; PHOSPHOSERINE PHOSPHATASE; 1.
DR   Pfam; PF13740; ACT_6; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SFLD; SFLDF00029; phosphoserine_phosphatase; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   PROSITE; PS51382; SPX; 1.
PE   3: Inferred from homology;
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:UP000265703};
KW   Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299}.
FT   DOMAIN          1..112
FT                   /note="SPX"
FT                   /evidence="ECO:0000259|PROSITE:PS51382"
FT   ACT_SITE        395
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604469-1"
FT   ACT_SITE        397
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604469-1"
SQ   SEQUENCE   610 AA;  68382 MW;  501D4FF562BFB71C CRC64;
     MSWKPSDSNE LHFIKLVSTR LSILQIKTTE FLEKLDNEIQ KVSDFFVKES NLLIKKSEEK
     NVDTFDENEA SKMLESIIRL ENFVFLSYTG LVKILKKHDK HSGLSIGEAY LYRTASLTLT
     KSDLLLILKK SLMEKVIQEV SPTSSKTTPT IINNGIKVEN NSTTTSSSVS LGTTTLPTLL
     SKIPQSTTSP TIKKNLFPPS NLLPHQKVIV SLTGPHGTDI IGCVLECMAK HDCEIEDFML
     SRLYHDVTFG VLITLNTHNI DLFRDLAEAS RKWDGTLAFD VHDRDQNYYT SSIEDAPYEN
     RIKYTATVLN QNGLTPQFLN DWTKFLLKEK ISVEKMQRLN EGKLSCADYK LSVPNNTDFE
     RLRQELFTLS TSHGTDVALQ PYDVFRRHKR LVVFDMDSTL IQQEVIDEIA RHAGVVNEVA
     AITELAMNGE IDFKESLRRR VALLKGTPVE VLQTVKENLT FTEGAHFLCK ALKKIGFKLA
     VISGGFIPLA KYVKNELGLD YAFANQLKVS SDGLTLTGET VGPIVDAERK AELLEVIAQA
     ENVTLDQVTA IGDGANDLLM LAKSGLGIAF NAKPRVQEKA RARINQKSLK YVLYLLGYTD
     EDAKQLYNDS
//
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