ART1B_SCHPO
ID ART1B_SCHPO Reviewed; 442 AA.
AC O94725;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Damage-control phosphatase SPCC1393.13 {ECO:0000250|UniProtKB:Q04371};
DE EC=3.1.3.- {ECO:0000250|UniProtKB:Q04371};
DE AltName: Full=Sugar phosphate phosphatase SPCC1393.13 {ECO:0000250|UniProtKB:Q04371};
GN ORFNames=SPCC1393.13;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: Metal-dependent phosphatase that shows phosphatase activity
CC against several substrates, including fructose-1-phosphate and
CC fructose-6-phosphate (By similarity). Its preference for fructose-1-
CC phosphate, a strong glycating agent that causes DNA damage rather than
CC a canonical yeast metabolite, suggests a damage-control function in
CC hexose phosphate metabolism (By similarity).
CC {ECO:0000250|UniProtKB:Q04371}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 1-phosphate + H2O = D-fructose + phosphate;
CC Xref=Rhea:RHEA:35603, ChEBI:CHEBI:15377, ChEBI:CHEBI:37721,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:138881;
CC Evidence={ECO:0000250|UniProtKB:Q04371};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 6-phosphate = D-glyceraldehyde 3-phosphate +
CC dihydroxyacetone; Xref=Rhea:RHEA:28002, ChEBI:CHEBI:16016,
CC ChEBI:CHEBI:57634, ChEBI:CHEBI:59776;
CC Evidence={ECO:0000250|UniProtKB:Q04371};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q04371};
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000250|UniProtKB:Q04371};
CC -!- DOMAIN: Subfamily III proteins have a conserved RTxK motif about 40-50
CC residues from the C-terminus; the threonine may be replaced by serine
CC or cysteine. {ECO:0000250|UniProtKB:Q04371}.
CC -!- SIMILARITY: Belongs to the damage-control phosphatase family. Sugar
CC phosphate phosphatase III subfamily. {ECO:0000305}.
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DR EMBL; CU329672; CAB38168.1; -; Genomic_DNA.
DR PIR; T40961; T40961.
DR RefSeq; NP_587971.1; NM_001022962.2.
DR AlphaFoldDB; O94725; -.
DR SMR; O94725; -.
DR BioGRID; 275411; 5.
DR STRING; 4896.SPCC1393.13.1; -.
DR iPTMnet; O94725; -.
DR MaxQB; O94725; -.
DR PaxDb; O94725; -.
DR PRIDE; O94725; -.
DR EnsemblFungi; SPCC1393.13.1; SPCC1393.13.1:pep; SPCC1393.13.
DR GeneID; 2538830; -.
DR KEGG; spo:SPCC1393.13; -.
DR PomBase; SPCC1393.13; -.
DR VEuPathDB; FungiDB:SPCC1393.13; -.
DR eggNOG; KOG3870; Eukaryota.
DR HOGENOM; CLU_030117_2_1_1; -.
DR InParanoid; O94725; -.
DR OMA; LFMEMCE; -.
DR PhylomeDB; O94725; -.
DR PRO; PR:O94725; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0097023; F:fructose 6-phosphate aldolase activity; IEA:RHEA.
DR GO; GO:0103026; F:fructose-1-phosphatase activity; IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR GO; GO:1990748; P:cellular detoxification; ISM:PomBase.
DR GO; GO:2001020; P:regulation of response to DNA damage stimulus; IBA:GO_Central.
DR InterPro; IPR036075; ARMT-1-like_metal-bd_sf.
DR InterPro; IPR039763; ARMT1.
DR InterPro; IPR002791; ARMT1-like_metal-bd.
DR PANTHER; PTHR12260; PTHR12260; 1.
DR Pfam; PF01937; ARMT1-like_dom; 1.
DR SUPFAM; SSF111321; SSF111321; 1.
PE 3: Inferred from homology;
KW Hydrolase; Manganese; Metal-binding; Nickel; Reference proteome.
FT CHAIN 1..442
FT /note="Damage-control phosphatase SPCC1393.13"
FT /id="PRO_0000230802"
FT MOTIF 402..405
FT /note="Subfamily III RTxK motif"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
FT BINDING 252..253
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
FT BINDING 252
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
FT BINDING 253
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
FT BINDING 290
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
FT BINDING 367..371
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
FT BINDING 405
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
SQ SEQUENCE 442 AA; 50117 MW; 8EEB6AABD1D9A306 CRC64;
MGLKLLHPPK PYAMTSDPES YASVCVMKKW PIIATNVIDE VSRNISKALE AGMSDKAAYV
TQGKEIISLL NQLKYDLQHN RPLKPLVGQG PDIDDYNEEL EQVGPLTWGD APWLYAGCYF
YRIMSLFFQA RSEWNRHDPF FEQKDFTLRS SKSAIEEFAK RYVHLNSELA SIQENKDDKA
AYMIFVEMAE ISLWGNAIDL GLLVNATYEQ LQSLQGQKAV EESQKNILVN DFPKIWSKLS
KVRHGRIDFV LDNAGFELFV DLLFATYLLK TEIAETIILH PKDVPWFVSD VLVNDIPHLF
NSLTSYFSGE GVQKLASDLA EFHAEGKIVI RPNPFWTTAH YFGRLPDVAP KLLSDLEQSD
MVIFKGDLNF RKLTGDCEWP HTTPFAEALG PIAGKFNILA LRTIKADVVV GLGKGVYEEI
AKDNPHWERT GKYAVVEFCP KD
