SERB_MYCA1
ID SERB_MYCA1 Reviewed; 411 AA.
AC A0QJI1;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Phosphoserine phosphatase;
DE Short=PSP;
DE Short=PSPase;
DE EC=3.1.3.3;
DE AltName: Full=O-phosphoserine phosphohydrolase;
GN Name=serB; OrderedLocusNames=MAV_3907;
OS Mycobacterium avium (strain 104).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=243243;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=104;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS,
RP COFACTOR, AND SUBUNIT.
RX PubMed=21359836; DOI=10.1007/s10969-011-9101-7;
RA Abendroth J., Gardberg A.S., Robinson J.I., Christensen J.S., Staker B.L.,
RA Myler P.J., Stewart L.J., Edwards T.E.;
RT "SAD phasing using iodide ions in a high-throughput structural genomics
RT environment.";
RL J. Struct. Funct. Genomics 12:83-95(2011).
CC -!- FUNCTION: Catalyzes the dephosphorylation of phosphoserine (P-Ser).
CC {ECO:0000250}.
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 -!- 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:21359836};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:21359836};
CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC 3-phospho-D-glycerate: step 3/3.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21359836}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. SerB family.
CC {ECO:0000305}.
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DR EMBL; CP000479; ABK66444.1; -; Genomic_DNA.
DR RefSeq; WP_011725747.1; NC_008595.1.
DR PDB; 3P96; X-ray; 2.05 A; A=1-411.
DR PDB; 5IS2; X-ray; 1.88 A; A=5-400.
DR PDB; 5IT0; X-ray; 1.97 A; A=5-400.
DR PDB; 5IT4; X-ray; 2.10 A; A=5-400.
DR PDB; 5JJB; X-ray; 2.31 A; A=5-400.
DR PDB; 5JLP; X-ray; 2.50 A; A=5-400.
DR PDB; 5JLR; X-ray; 2.26 A; A=5-400.
DR PDB; 5JMA; X-ray; 2.03 A; A=5-400.
DR PDB; 5T41; X-ray; 3.15 A; A=5-400.
DR PDBsum; 3P96; -.
DR PDBsum; 5IS2; -.
DR PDBsum; 5IT0; -.
DR PDBsum; 5IT4; -.
DR PDBsum; 5JJB; -.
DR PDBsum; 5JLP; -.
DR PDBsum; 5JLR; -.
DR PDBsum; 5JMA; -.
DR PDBsum; 5T41; -.
DR AlphaFoldDB; A0QJI1; -.
DR SMR; A0QJI1; -.
DR EnsemblBacteria; ABK66444; ABK66444; MAV_3907.
DR KEGG; mav:MAV_3907; -.
DR HOGENOM; CLU_036368_1_1_11; -.
DR OMA; FAAHAGC; -.
DR OrthoDB; 1755462at2; -.
DR UniPathway; UPA00135; UER00198.
DR EvolutionaryTrace; A0QJI1; -.
DR Proteomes; UP000001574; Chromosome.
DR GO; GO:0036424; F:L-phosphoserine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1000; -; 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 SFLD; SFLDF00029; phosphoserine_phosphatase; 1.
DR SUPFAM; SSF55021; SSF55021; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR00338; serB; 1.
DR PROSITE; PS51671; ACT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Hydrolase; Magnesium; Metal-binding;
KW Serine biosynthesis.
FT CHAIN 1..411
FT /note="Phosphoserine phosphatase"
FT /id="PRO_0000401184"
FT DOMAIN 10..88
FT /note="ACT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT ACT_SITE 187
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 189
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:21359836,
FT ECO:0007744|PDB:3P96"
FT BINDING 189
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:21359836,
FT ECO:0007744|PDB:3P96"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 275..276
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 320
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 343
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:21359836,
FT ECO:0007744|PDB:3P96"
FT BINDING 346
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT STRAND 7..16
FT /evidence="ECO:0007829|PDB:5IS2"
FT HELIX 21..30
FT /evidence="ECO:0007829|PDB:5IS2"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:5IS2"
FT STRAND 35..44
FT /evidence="ECO:0007829|PDB:5IS2"
FT STRAND 47..56
FT /evidence="ECO:0007829|PDB:5IS2"
FT HELIX 58..61
FT /evidence="ECO:0007829|PDB:5IS2"
FT HELIX 64..76
FT /evidence="ECO:0007829|PDB:5IS2"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:5IS2"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:5IS2"
FT STRAND 97..106
FT /evidence="ECO:0007829|PDB:5IS2"
FT HELIX 109..121
FT /evidence="ECO:0007829|PDB:5IS2"
FT STRAND 125..145
FT /evidence="ECO:0007829|PDB:5IS2"
FT HELIX 151..165
FT /evidence="ECO:0007829|PDB:5IS2"
FT STRAND 168..173
FT /evidence="ECO:0007829|PDB:5IS2"
FT TURN 176..179
FT /evidence="ECO:0007829|PDB:5IS2"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:5IS2"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:5IS2"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:5IS2"
FT HELIX 197..204
FT /evidence="ECO:0007829|PDB:5IS2"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:5IS2"
FT HELIX 214..219
FT /evidence="ECO:0007829|PDB:5IS2"
FT HELIX 225..234
FT /evidence="ECO:0007829|PDB:5IS2"
FT TURN 235..238
FT /evidence="ECO:0007829|PDB:5IS2"
FT HELIX 242..248
FT /evidence="ECO:0007829|PDB:5IS2"
FT HELIX 257..266
FT /evidence="ECO:0007829|PDB:5IS2"
FT STRAND 270..278
FT /evidence="ECO:0007829|PDB:5IS2"
FT HELIX 279..288
FT /evidence="ECO:0007829|PDB:5IS2"
FT STRAND 292..297
FT /evidence="ECO:0007829|PDB:5IS2"
FT STRAND 299..302
FT /evidence="ECO:0007829|PDB:5IS2"
FT STRAND 305..310
FT /evidence="ECO:0007829|PDB:5IS2"
FT HELIX 317..331
FT /evidence="ECO:0007829|PDB:5IS2"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:5IS2"
FT STRAND 338..342
FT /evidence="ECO:0007829|PDB:5IS2"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:5IS2"
FT HELIX 348..353
FT /evidence="ECO:0007829|PDB:5IS2"
FT STRAND 354..361
FT /evidence="ECO:0007829|PDB:5IS2"
FT HELIX 364..367
FT /evidence="ECO:0007829|PDB:5IS2"
FT STRAND 370..374
FT /evidence="ECO:0007829|PDB:5IS2"
FT HELIX 381..385
FT /evidence="ECO:0007829|PDB:5IS2"
FT HELIX 390..399
FT /evidence="ECO:0007829|PDB:5IS2"
SQ SEQUENCE 411 AA; 43339 MW; 2BBB69EBBDE7D022 CRC64;
MNSPPKVSVL ITVTGVDQPG VTATLFEVLS GHGVELLNVE QVVIRHRLTL GVLVCCPADV
ADGPALRHDV EAAIRKVGLD VSIERSDDVP IIREPSTHTI FVLGRPITAA AFGAVAREVA
ALGVNIDLIR GVSDYPVIGL ELRVSVPPGA DGALRTALNR VSSEEHVDVA VEDYTLERRA
KRLIVFDVDS TLVQGEVIEM LAAKAGAEGQ VAAITDAAMR GELDFAQSLQ QRVATLAGLP
ATVIDEVAGQ LELMPGARTT LRTLRRLGYA CGVVSGGFRR IIEPLAEELM LDYVAANELE
IVDGTLTGRV VGPIIDRAGK ATALREFAQR AGVPMAQTVA VGDGANDIDM LAAAGLGIAF
NAKPALREVA DASLSHPYLD TVLFLLGVTR GEIEAADAID GEVRRVEIPP E
