ID   I0GPK5_SELRL            Unreviewed;       438 AA.
AC   I0GPK5;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=Putative glucose-1-phosphatase {ECO:0000313|EMBL:BAL82692.1};
DE            EC=3.1.3.10 {ECO:0000313|EMBL:BAL82692.1};
GN   Name=agp {ECO:0000313|EMBL:BAL82692.1};
GN   OrderedLocusNames=SELR_09840 {ECO:0000313|EMBL:BAL82692.1};
OS   Selenomonas ruminantium subsp. lactilytica (strain NBRC 103574 / TAM6421).
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC   Selenomonas.
OX   NCBI_TaxID=927704 {ECO:0000313|EMBL:BAL82692.1, ECO:0000313|Proteomes:UP000007887};
RN   [1] {ECO:0000313|EMBL:BAL82692.1, ECO:0000313|Proteomes:UP000007887}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 103574 / TAM6421 {ECO:0000313|Proteomes:UP000007887};
RA   Oguchi A., Ankai A., Kaneko J., Yamada-Narita S., Fukui S., Takahashi M.,
RA   Onodera T., Kojima S., Fushimi T., Abe N., Kamio Y., Yamazaki S.,
RA   Fujita N.;
RT   "Whole genome sequence of Selenomonas ruminantium subsp. lactilytica
RT   TAM6421.";
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC       {ECO:0000256|ARBA:ARBA00005375}.
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DR   EMBL; AP012292; BAL82692.1; -; Genomic_DNA.
DR   AlphaFoldDB; I0GPK5; -.
DR   KEGG; sri:SELR_09840; -.
DR   PATRIC; fig|927704.6.peg.1014; -.
DR   eggNOG; ENOG502Z7K9; Bacteria.
DR   HOGENOM; CLU_030561_2_1_9; -.
DR   Proteomes; UP000007887; Chromosome.
DR   GO; GO:0008877; F:glucose-1-phosphatase activity; IEA:UniProtKB-EC.
DR   CDD; cd07061; HP_HAP_like; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 2.
DR   InterPro; IPR033379; Acid_Pase_AS.
DR   InterPro; IPR000560; His_Pase_clade-2.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   PANTHER; PTHR11567:SF110; ACID PHOSPHATASE 1, ISOFORM B; 1.
DR   PANTHER; PTHR11567; ACID PHOSPHATASE-RELATED; 1.
DR   Pfam; PF00328; His_Phos_2; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR   PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
DR   PROSITE; PS00778; HIS_ACID_PHOSPHAT_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:BAL82692.1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..438
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003626964"
SQ   SEQUENCE   438 AA;  48982 MW;  AB120C65A57E97D9 CRC64;
     MTMNLKKMAA SICLAMLTLS SVVQAERPAD FQDKYQLEEM VVLSRHNIRS PLSGNGSALG
     NLTPHAWFKW TSGPSELSLR GGQLETMMGQ YFRQRLVKDG LMTENYLPKE GEMRFYANSM
     QRTIATAQYF SSGMLPVANV KIEHKYAPSK MDPVFNPQLT FVSDAFRSQA MKEISAMGGK
     NGLQGINDKL NGEYRTLEKA LDLKDSPMAK KDGFSRFKND DLQIMLEVNK EPAMKGSLKL
     ANSASDAFIL QYYEEPDTTK AGFGHKLTQQ EWEQIASVKD VYGDVLFTAP SVAVNVAHPL
     LKEMQNELAQ PGRKFTFLCG HDSNIASVLA ALDVEEYSLP NSIEKKTPIG SKLVIEKFAG
     KDGKEYAAMS LVYQNPEQLR DRTALTLDNP PEIFPLKLKG MKTNVDGVYR LKDVQQRFEQ
     AIKAYDKLPQ DKAEKKAA
//