Y328_SYNY3
ID Y328_SYNY3 Reviewed; 157 AA.
AC Q55535;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Putative low molecular weight protein-tyrosine-phosphatase slr0328;
DE EC=3.1.3.48;
GN OrderedLocusNames=slr0328;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA Sugiura M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT from map positions 64% to 92% of the genome.";
RL DNA Res. 2:153-166(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48;
CC -!- SIMILARITY: Belongs to the low molecular weight phosphotyrosine protein
CC phosphatase family. {ECO:0000305}.
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DR EMBL; BA000022; BAA10030.1; -; Genomic_DNA.
DR PIR; S76052; S76052.
DR PDB; 5O7B; X-ray; 2.28 A; A=2-157.
DR PDBsum; 5O7B; -.
DR AlphaFoldDB; Q55535; -.
DR SMR; Q55535; -.
DR STRING; 1148.1001408; -.
DR PaxDb; Q55535; -.
DR EnsemblBacteria; BAA10030; BAA10030; BAA10030.
DR KEGG; syn:slr0328; -.
DR eggNOG; COG0394; Bacteria.
DR InParanoid; Q55535; -.
DR OMA; TGSWHVG; -.
DR PhylomeDB; Q55535; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR InterPro; IPR023485; Ptyr_pPase.
DR InterPro; IPR036196; Ptyr_pPase_sf.
DR InterPro; IPR017867; Tyr_phospatase_low_mol_wt.
DR Pfam; PF01451; LMWPc; 1.
DR PRINTS; PR00719; LMWPTPASE.
DR SMART; SM00226; LMWPc; 1.
DR SUPFAM; SSF52788; SSF52788; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Protein phosphatase; Reference proteome.
FT CHAIN 1..157
FT /note="Putative low molecular weight protein-tyrosine-
FT phosphatase slr0328"
FT /id="PRO_0000046581"
FT ACT_SITE 7
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P11064"
FT ACT_SITE 13
FT /evidence="ECO:0000250|UniProtKB:P11064"
FT ACT_SITE 124
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P11064"
FT STRAND 4..12
FT /evidence="ECO:0007829|PDB:5O7B"
FT HELIX 13..24
FT /evidence="ECO:0007829|PDB:5O7B"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:5O7B"
FT TURN 44..47
FT /evidence="ECO:0007829|PDB:5O7B"
FT HELIX 52..55
FT /evidence="ECO:0007829|PDB:5O7B"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:5O7B"
FT HELIX 88..91
FT /evidence="ECO:0007829|PDB:5O7B"
FT HELIX 130..143
FT /evidence="ECO:0007829|PDB:5O7B"
SQ SEQUENCE 157 AA; 17470 MW; D642D8E6D3A49751 CRC64;
MKLLFVCLGN ICRSPAAENI MNAQIDQAGL GAKIVCDSAG TSSYHVGDSP DRRMTESLKK
RGYRVQGRAR QFFPEDFAEF DLILAMDGDN YRNILAQDPA GQYHHKVKMI CDYTEKFGDR
EVPDPYYGGQ AGFEHVIDLL EDACGNLLTS LGKELVN