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Database: UniProt
Entry: A1UE42_MYCSK
LinkDB: A1UE42_MYCSK
Original site: A1UE42_MYCSK 
ID   A1UE42_MYCSK            Unreviewed;       417 AA.
AC   A1UE42;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   24-JAN-2024, entry version 91.
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   OrderedLocusNames=Mkms_1900 {ECO:0000313|EMBL:ABL91100.1};
OS   Mycobacterium sp. (strain KMS).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=189918 {ECO:0000313|EMBL:ABL91100.1};
RN   [1] {ECO:0000313|EMBL:ABL91100.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KMS {ECO:0000313|EMBL:ABL91100.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.D.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium sp. KMS.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001197};
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:0000256|ARBA:ARBA00000860};
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; CP000518; ABL91100.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1UE42; -.
DR   STRING; 189918.Mkms_1900; -.
DR   KEGG; mkm:Mkms_1900; -.
DR   HOGENOM; CLU_036368_1_2_11; -.
DR   OMA; FAAHAGC; -.
DR   OrthoDB; 9792539at2; -.
DR   UniPathway; UPA00135; UER00198.
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; cd04870; ACT_PSP_1; 1.
DR   Gene3D; 3.30.70.260; -; 2.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR004469; PSP.
DR   InterPro; IPR049148; PSP_ACT.
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; PF21086; ACT_PSP_2; 1.
DR   Pfam; PF12710; HAD; 1.
DR   SFLD; SFLDG01136; C1.6:_Phosphoserine_Phosphatas; 1.
DR   SFLD; SFLDF00029; phosphoserine_phosphatase; 1.
DR   SUPFAM; SSF55021; ACT-like; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   PROSITE; PS51671; ACT; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023299};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ABL91100.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299}.
FT   DOMAIN          15..93
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   ACT_SITE        193
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604469-1"
FT   ACT_SITE        195
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604469-1"
SQ   SEQUENCE   417 AA;  44084 MW;  BC1AB700DC9C849E CRC64;
     MTSPVGSSRK RSSLLITVTG VDQPGVTSAL FEVLSRHRVE LLNVEQVVIR GRLTLGVLVA
     AAPEVADGDG LRTDVEEAIH DVGLDVTIER SADTPVMREP STHTIVVLGR PITAEAFGVV
     AREVAALGVN IDTIRGVSDY PVTGLELRVS VPAGAAYGQL QKAMARVAVA EGVDIALEDY
     SLSRRAKRLI VFDVDSTLIQ GEVIEMLAAR AGAEAAVAEV TEAAMRGELD FAESLHRRVA
     TLAGLPASVL DDVADQIELT AGARTTLRTL RRLGFHCGIV SGGFRQVIEP LAHELMMDFV
     AANELEIVDG KLTGRVVGEV IDRPGKAKAL RDFAQQAGVP MEQTVAVGDG ANDIDMLSAA
     GLGVAFNAKP ALREVADASL SHPYLDTVLF ILGVTRGEIE AADAVDGLLR RVEIPED
//
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