inositol-1-monophosphatase [Vibrio splendidus].

LOCUS       WP_004740344             267 aa            linear   BCT 15-MAY-2023
ACCESSION   WP_004740344
VERSION     WP_004740344.1
KEYWORDS    RefSeq.
SOURCE      Vibrio splendidus
  ORGANISM  Vibrio splendidus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Huang,Y.H., Hilal,T., Loll,B., Burger,J., Mielke,T., Bottcher,C.,
            Said,N. and Wahl,M.C.
  TITLE     Structure-Based Mechanisms of a Molecular RNA Polymerase/Chaperone
            Machine Required for Ribosome Biosynthesis
  JOURNAL   Mol Cell 79 (6), 1024-1036 (2020)
   PUBMED   32871103
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Chen,L. and Roberts,M.F.
  TITLE     Overexpression, purification, and analysis of complementation
            behavior of E. coli SuhB protein: comparison with bacterial and
            archaeal inositol monophosphatases
  JOURNAL   Biochemistry 39 (14), 4145-4153 (2000)
   PUBMED   10747806
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF008027.1
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK10757
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Vibrio splendidus"
                     /db_xref="taxon:29497"
     gene            1..267
                     /gene="suhB"
     Protein         1..267
                     /product="inositol-1-monophosphatase"
                     /EC_number="3.1.3.25"
                     /GO_function="GO:0008934 - inositol monophosphate
                     1-phosphatase activity [Evidence IEA]"
                     /GO_process="GO:0046854 - phosphatidylinositol phosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=29060
     Region          1..265
                     /region_name="FIG"
                     /note="FBPase/IMPase/glpX-like domain. A superfamily of
                     metal-dependent phosphatases with various substrates.
                     Fructose-1,6-bisphospatase (both the major and the
                     glpX-encoded variant) hydrolyze fructose-1,6,-bisphosphate
                     to fructose-6-phosphate in...; cl00289"
                     /db_xref="CDD:469707"
     Site            order(33,38,44,67..68,84..89,211..212)
                     /site_type="active"
                     /db_xref="CDD:238817"
     Site            order(37,39,90..91,93..98,150..152,154,156..157,165..166,
                     169,172..173,176,180..186,194,198..201)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238817"
ORIGIN      
        1 mhpmlniair aarkagnhia kslettdkie tslkgnndyv tniaqeaeym iietikasyp
       61 ehsiiseekg liegkdsdvq wivdpldgtn nfvkgfphfs vsiavrmngr tevacvydpm
      121 lnelftaqrg agaqlnnarm rvtqlkdlqg svlatgfpfk akqhsesfmk iisglfvdcs
      181 dfrrtgspal dlcylaagrv dgyleldlkp wdmaagdlia reagailtdf sggtdymksg
      241 nvvassargv kailkhvren anegmlk