ID B6SEG5_9ACTN Unreviewed; 306 AA. AC B6SEG5; DT 16-DEC-2008, integrated into UniProtKB/TrEMBL. DT 16-DEC-2008, sequence version 1. DT 27-MAR-2024, entry version 57. DE SubName: Full=AlnA {ECO:0000313|EMBL:ACI88875.1}; GN Name=alnA {ECO:0000313|EMBL:ACI88875.1}; OS Streptomyces sp. CM020. OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces. OX NCBI_TaxID=569580 {ECO:0000313|EMBL:ACI88875.1}; RN [1] {ECO:0000313|EMBL:ACI88875.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CM020 {ECO:0000313|EMBL:ACI88875.1}; 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:4EX8, ECO:0007829|PDB:4EX9} RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 2-306 IN COMPLEX WITH CALCIUM. 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). CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; EU852062; ACI88875.1; -; Genomic_DNA. DR PDB; 4EX8; X-ray; 2.10 A; A=2-306. DR PDB; 4EX9; X-ray; 3.15 A; A=2-306. DR PDBsum; 4EX8; -. DR PDBsum; 4EX9; -. DR AlphaFoldDB; B6SEG5; -. DR SMR; B6SEG5; -. DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004730; F:pseudouridylate synthase activity; IEA:InterPro. DR Gene3D; 3.40.1790.10; Indigoidine synthase domain; 1. DR InterPro; IPR022830; Indigdn_synthA-like. DR InterPro; IPR007342; PsuG. DR PANTHER; PTHR42909:SF1; PFKB DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR42909; ZGC:136858; 1. DR Pfam; PF04227; Indigoidine_A; 1. DR SUPFAM; SSF110581; Indigoidine synthase A-like; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:4EX8, ECO:0007829|PDB:4EX9}; KW Calcium {ECO:0007829|PDB:4EX8, ECO:0007829|PDB:4EX9}; KW Glycosidase {ECO:0000256|ARBA:ARBA00023295}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Lyase {ECO:0000256|ARBA:ARBA00023239}; KW Manganese {ECO:0000256|ARBA:ARBA00023211}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0007829|PDB:4EX8}. FT BINDING 29 FT /ligand="D-ribulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:58121" FT /evidence="ECO:0007829|PDB:4EX9" FT BINDING 106 FT /ligand="D-ribulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:58121" FT /evidence="ECO:0007829|PDB:4EX9" FT BINDING 130 FT /ligand="D-ribulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:58121" FT /evidence="ECO:0007829|PDB:4EX9" FT BINDING 135 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4EX8, ECO:0007829|PDB:4EX9" FT BINDING 138 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4EX8, ECO:0007829|PDB:4EX9" FT BINDING 140 FT /ligand="D-ribulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:58121" FT /evidence="ECO:0007829|PDB:4EX9" FT BINDING 142 FT /ligand="D-ribulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:58121" FT /evidence="ECO:0007829|PDB:4EX9" FT BINDING 159 FT /ligand="D-ribulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:58121" FT /evidence="ECO:0007829|PDB:4EX9" FT BINDING 169 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4EX8, ECO:0007829|PDB:4EX9" FT BINDING 172 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4EX8, ECO:0007829|PDB:4EX9" SQ SEQUENCE 306 AA; 31633 MW; 9509703572DAE228 CRC64; MERQPDQLLE VSDEIATALA ERRPVVALES SLITTDPSSE TASLIEKAVR GAGAVPATIG IAGGKLVVGL TDSLIERFAS TKGIPKISAR DIGGALAGGG LGATTVAGTI VIAERAGIQV FTTAGIGGVH RRGEDTLDIS PDLLQFRKTK MTVVSGGAKS ILDHRLTAEY LETAGVPVYG YRTDKLAAFV VREADVPVTR MDDLHTAARA AEAHWQVNGP GTVLLTSPID EQDAVDEAIV EAAIAEALAQ CDQEGIVGNA VSPYLMKALA RASGGMLPKA GRSLLLSTAR VAGEFSAALS AVQAER //