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Database: UniProt
Entry: A0A1Q3SH80_9CHLR
LinkDB: A0A1Q3SH80_9CHLR
Original site: A0A1Q3SH80_9CHLR 
ID   A0A1Q3SH80_9CHLR        Unreviewed;       337 AA.
AC   A0A1Q3SH80;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Metalloenzyme domain-containing protein {ECO:0000259|Pfam:PF01676};
GN   ORFNames=BGO39_17610 {ECO:0000313|EMBL:OJV88462.1};
OS   Chloroflexi bacterium 54-19.
OC   Bacteria; Chloroflexota.
OX   NCBI_TaxID=1895928 {ECO:0000313|EMBL:OJV88462.1, ECO:0000313|Proteomes:UP000186384};
RN   [1] {ECO:0000313|EMBL:OJV88462.1, ECO:0000313|Proteomes:UP000186384}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=54-19 {ECO:0000313|EMBL:OJV88462.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SIMILARITY: Belongs to the phosphopentomutase family.
CC       {ECO:0000256|ARBA:ARBA00010373}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OJV88462.1}.
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DR   EMBL; MKTJ01000081; OJV88462.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q3SH80; -.
DR   STRING; 1895928.BGO39_17610; -.
DR   Proteomes; UP000186384; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0008973; F:phosphopentomutase activity; IEA:InterPro.
DR   GO; GO:0043094; P:cellular metabolic compound salvage; IEA:InterPro.
DR   GO; GO:0009117; P:nucleotide metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR010045; DeoB.
DR   InterPro; IPR006124; Metalloenzyme.
DR   PANTHER; PTHR21110; PHOSPHOPENTOMUTASE; 1.
DR   PANTHER; PTHR21110:SF0; PHOSPHOPENTOMUTASE; 1.
DR   Pfam; PF01676; Metalloenzyme; 1.
DR   SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE   3: Inferred from homology;
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          220..317
FT                   /note="Metalloenzyme"
FT                   /evidence="ECO:0000259|Pfam:PF01676"
SQ   SEQUENCE   337 AA;  36796 MW;  C61014DF10E4DD45 CRC64;
     MPDHRPSFYK KGIPLAELSA NRFIYLFLDG IGLAPAGPDN PFSPGEETPD DPGPMPFLAG
     LLDGPLLAGP PILTEDLLFK PVDATLGVPG RPQSATGQTA LYTGRNAPEF LGRHLTGFAN
     GSLRILIEES GLFKQVLALG GRPTAANLYT PEYFQAIENR RLRYSVGALL NLTSGVPFRM
     PENYEREEAL FWDITNRYSR SRGFSLPLIS PQEAGRRLAN LAAKYDVTLF ESYLPDYAGH
     AQDKQRALSI LQEVDGLIEG IMRYKSVETS LVICSDHGNL ENLASKLHTL NPVPLLVFGP
     AAPAFAQVDT IMGLTPVIVE QIRLGQADRK DLKPGLN
//
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