ID   M1PAS_EIMTE             Reviewed;         309 AA.
AC   O43980;
DT   11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Mannitol-1-phosphatase;
DE            Short=M1Pase;
DE            EC=3.1.3.22;
OS   Eimeria tenella (Coccidian parasite).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX   NCBI_TaxID=5802;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 20-30; 67-81;
RP   93-117; 128-132; 142-158; 160-175; 177-187; 205-214 AND 282-293, FUNCTION,
RP   CATALYTIC ACTIVITY, ENZYME REACTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=9461622; DOI=10.1074/jbc.273.7.4237;
RA   Liberator P., Anderson J., Feiglin M., Sardana M., Griffin P., Schmatz D.,
RA   Myers R.W.;
RT   "Molecular cloning and functional expression of mannitol-1-phosphatase from
RT   the apicomplexan parasite Eimeria tenella.";
RL   J. Biol. Chem. 273:4237-4244(1998).
CC   -!- FUNCTION: Key enzyme for mannitol biosynthesis.
CC       {ECO:0000269|PubMed:9461622}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-mannitol 1-phosphate + H2O = D-mannitol + phosphate;
CC         Xref=Rhea:RHEA:19537, ChEBI:CHEBI:15377, ChEBI:CHEBI:16899,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:61381; EC=3.1.3.22;
CC         Evidence={ECO:0000269|PubMed:9461622};
CC   -!- ACTIVITY REGULATION: By diethyl pyrocarbonate (DEPC).
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=69 uM for D-mannitol 1-phosphate {ECO:0000269|PubMed:9461622};
CC         Vmax=953 umol/min/mg enzyme {ECO:0000269|PubMed:9461622};
CC         Note=kcat is 550 sec(-1).;
CC   -!- SIMILARITY: Belongs to the phosphoglycerate mutase family.
CC       {ECO:0000305}.
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DR   EMBL; AF032462; AAC38954.1; -; mRNA.
DR   AlphaFoldDB; O43980; -.
DR   SMR; O43980; -.
DR   VEuPathDB; ToxoDB:ETH2_0825200; -.
DR   VEuPathDB; ToxoDB:ETH_00027300; -.
DR   BioCyc; MetaCyc:MON-15724; -.
DR   GO; GO:0050084; F:mannitol-1-phosphatase activity; IDA:UniProtKB.
DR   GO; GO:0019593; P:mannitol biosynthetic process; IDA:UniProtKB.
DR   Gene3D; 3.40.50.1240; -; 1.
DR   InterPro; IPR013078; His_Pase_superF_clade-1.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   Pfam; PF00300; His_Phos_1; 1.
DR   SMART; SM00855; PGAM; 1.
DR   SUPFAM; SSF53254; SSF53254; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase.
FT   CHAIN           1..309
FT                   /note="Mannitol-1-phosphatase"
FT                   /id="PRO_0000418463"
FT   ACT_SITE        82
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P62707"
FT   ACT_SITE        166
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P62707"
SQ   SEQUENCE   309 AA;  34737 MW;  DAEAF59ECA96C748 CRC64;
     MAETEWTPEA LSGRYEEIKS CIPQQLEAYA RFLREAAPED LRRWQQIAQD LKLELNLENG
     RIKYKKEFKP LELPVDICYI RHGKTQGNTE PRVFQGQVDY ANNQLTQQGQ QQAAAAATKL
     EAMAAAKEFI PDLLLSSPLL RAVHTAQPFV DANPKPLFRV LPELAEMAFG EWDNRKVAEL
     EKDDPAHLFY LQQNAVIKAK GPHRICCQLW QSPEWLEGKK ELPAENFLEC LDRQRKALIK
     VGEIAKELCG PSCGERKPRV AVYGHSMAGA AVSVLLGFGK EDQLGFLGFD GNYIMPNATP
     TILIPNAKP