ID   B6SEG4_9ACTN            Unreviewed;       227 AA.
AC   B6SEG4;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=AlnB {ECO:0000313|EMBL:ACI88874.1};
GN   Name=alnB {ECO:0000313|EMBL:ACI88874.1};
OS   Streptomyces sp. CM020.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=569580 {ECO:0000313|EMBL:ACI88874.1};
RN   [1] {ECO:0000313|EMBL:ACI88874.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CM020 {ECO:0000313|EMBL:ACI88874.1};
RX   PubMed=18940666; DOI=10.1016/j.chembiol.2008.07.022;
RA   Oja T., Palmu K., Lehmussola H., Lepparanta O., Hannikainen K., Niemi J.,
RA   Mantsala P., Metsa-Ketela M.;
RT   "Characterization of the alnumycin gene cluster reveals unusual gene
RT   products for pyran ring formation and dioxan biosynthesis.";
RL   Chem. Biol. 15:1046-1057(2008).
RN   [2] {ECO:0007829|PDB:4EX6, ECO:0007829|PDB:4EX7}
RP   X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 2-227 IN COMPLEX WITH MAGNESIUM.
RX   PubMed=23297194; DOI=10.1073/pnas.1207407110;
RA   Oja T., Niiranen L., Sandalova T., Klika K.D., Niemi J., Mantsala P.,
RA   Schneider G., Metsa-Ketela M.;
RT   "Structural basis for C-ribosylation in the alnumycin A biosynthetic
RT   pathway.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:1291-1296(2013).
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DR   EMBL; EU852062; ACI88874.1; -; Genomic_DNA.
DR   PDB; 4EX6; X-ray; 1.25 A; A=2-227.
DR   PDB; 4EX7; X-ray; 1.50 A; A=2-227.
DR   PDBsum; 4EX6; -.
DR   PDBsum; 4EX7; -.
DR   AlphaFoldDB; B6SEG4; -.
DR   SMR; B6SEG4; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006439; HAD-SF_hydro_IA.
DR   InterPro; IPR041492; HAD_2.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR023198; PGP-like_dom2.
DR   NCBIfam; TIGR01549; HAD-SF-IA-v1; 1.
DR   NCBIfam; TIGR01509; HAD-SF-IA-v3; 1.
DR   PANTHER; PTHR43434:SF24; HYDROLASE-RELATED; 1.
DR   PANTHER; PTHR43434; PHOSPHOGLYCOLATE PHOSPHATASE; 1.
DR   Pfam; PF13419; HAD_2; 1.
DR   SFLD; SFLDG01135; C1.5.6:_HAD__Beta-PGM__Phospha; 1.
DR   SFLD; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:4EX6, ECO:0007829|PDB:4EX7};
KW   Metal-binding {ECO:0007829|PDB:4EX6, ECO:0007829|PDB:4EX7}.
FT   BINDING         15
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0007829|PDB:4EX6, ECO:0007829|PDB:4EX7"
FT   BINDING         17
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0007829|PDB:4EX6, ECO:0007829|PDB:4EX7"
FT   BINDING         175
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0007829|PDB:4EX6, ECO:0007829|PDB:4EX7"
SQ   SEQUENCE   227 AA;  22947 MW;  22A75EA575723B37 CRC64;
     MSGAPAAADR GVILDLDGTL ADTPAAIATI TAEVLAAMGT AVSRGAILST VGRPLPASLA
     GLLGVPVEDP RVAEATEEYG RRFGAHVRAA GPRLLYPGVL EGLDRLSAAG FRLAMATSKV
     EKAARAIAEL TGLDTRLTVI AGDDSVERGK PHPDMALHVA RGLGIPPERC VVIGDGVPDA
     EMGRAAGMTV IGVSYGVSGP DELMRAGADT VVDSFPAAVT AVLDGHP
//