ID A0A2T4B5M6_9HYPO Unreviewed; 485 AA.
AC A0A2T4B5M6;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=BBK36DRAFT_1122894 {ECO:0000313|EMBL:PTB64642.1};
OS Trichoderma citrinoviride.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=58853 {ECO:0000313|EMBL:PTB64642.1, ECO:0000313|Proteomes:UP000241546};
RN [1] {ECO:0000313|Proteomes:UP000241546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TUCIM 6016 {ECO:0000313|Proteomes:UP000241546};
RG DOE Joint Genome Institute;
RA Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B., Kuo A.,
RA Aerts A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y.,
RA Rahimi M.J., Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT "Multiple horizontal gene transfer events from other fungi enriched the
RT ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT plant biomass.";
RL Submitted (JUL-2016) 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}.
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DR EMBL; KZ680216; PTB64642.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T4B5M6; -.
DR OrthoDB; 789at2759; -.
DR UniPathway; UPA00135; UER00198.
DR Proteomes; UP000241546; 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 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 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; PF12710; HAD; 1.
DR SFLD; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 1.
DR SFLD; SFLDG01136; C1.6:_Phosphoserine_Phosphatas; 1.
DR SFLD; SFLDF00029; phosphoserine_phosphatase; 1.
DR SUPFAM; SSF56784; HAD-like; 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:UP000241546};
KW Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299}.
FT REGION 1..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 270
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR604469-1"
FT ACT_SITE 272
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR604469-1"
SQ SEQUENCE 485 AA; 53072 MW; AEBE6951629CB7D9 CRC64;
MADAATAKAP SQRPQLTSSM RSSSYLSDHQ QYRPPQHRIP EAHHGIDTLV EDASPSKSPK
LPFNGVPSPE HPPVVVDSGV SHSYSHPNCA PPAGRKSDRL IATLFYKGAD RSAPARSTSG
GLSRSRSPAS KNGGLADSTE SLPPNMAPTT SMDEFPLEPP THESAEPQLD HLYGSYVSPL
CITSFLHLMS TFPLPDDAEE PHSSHRCLDN QENPRVVELT LTPAPSPSYL SLADLRKHEL
IYRFEQEWNV DVALQRDTLW RKHPRLVVFD MDSTLITQEV IDLLAENLSD PPDLAERVAN
ITHRAMMGEL NFESSFRERV ALLKGLPATV FEGLRPVLNV TNGVRELLKA LKRLGVKTAV
LSGGFLPLTG WLAKELGIDY AHANEVVIED GKLTGEVKGI IVGKERKRDL LVEIAQKEGI
DLSQVIAVGD GANDLLMMEK AGLGVAWNAK PTVQMEADAR LNGQSLLDLL YLFGFTGEEI
DMLIS
//
