MULTISPECIES: imidazolonepropionase [Klebsiella].

LOCUS       WP_004153329             439 aa            linear   BCT 02-JUN-2024
ACCESSION   WP_004153329
VERSION     WP_004153329.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Tyagi,R., Kumaran,D., Burley,S.K. and Swaminathan,S.
  TITLE     X-ray structure of imidazolonepropionase from Agrobacterium
            tumefaciens at 1.87 A resolution
  JOURNAL   Proteins 69 (3), 652-658 (2007)
   PUBMED   17640072
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Yu,Y., Liang,Y.H., Brostromer,E., Quan,J.M., Panjikar,S., Dong,Y.H.
            and Su,X.D.
  TITLE     A catalytic mechanism revealed by the crystal structures of the
            imidazolonepropionase from Bacillus subtilis
  JOURNAL   J Biol Chem 281 (48), 36929-36936 (2006)
   PUBMED   16990261
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 :: TIGR01224.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     gene            1..439
                     /gene="hutI"
     Protein         1..439
                     /product="imidazolonepropionase"
                     /EC_number="3.5.2.7"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0016812 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in cyclic amides
                     [Evidence IEA]"
                     /GO_function="GO:0050480 - imidazolonepropionase activity
                     [Evidence IEA]"
                     /GO_process="GO:0019556 - histidine catabolic process to
                     glutamate and formamide [Evidence IEA]"
                     /calculated_mol_wt=47851
     Region          65..438
                     /region_name="metallo-dependent_hydrolases"
                     /note="Superfamily of metallo-dependent hydrolases (also
                     called amidohydrolase superfamily) is a large group of
                     proteins that show conservation in their 3-dimensional
                     fold (TIM barrel) and in details of their active site. The
                     vast majority of the members have a...; cl00281"
                     /db_xref="CDD:469705"
     Site            order(106,108,276,279,299,351)
                     /site_type="active"
                     /db_xref="CDD:238621"
ORIGIN      
        1 mvfshkkitf pcaivdftgv mkinvytthd klsamteats elviwrngrl atlnpdhaqp
       61 ygllerhall vrdgriaaiv aeddvpsgrs idlegrlvtp glidchthlv fggsraqewe
      121 qrlngvsyqt isasgggins tvratrdsse aellalaqpr lerllregvt tleiksgygl
      181 dlpnerkmlr varqladhng velsatllsa hatppeyqgd adgyitlvce tilptlwqeg
      241 lfesvdvfce nvgfspqqte rvfqaaqalg ipvkghveql sslggaqlvs ryhglsadhi
      301 eylteegvaa mresgtvaal lpgafyflne trkppvellr kyqvpmavat dfnpgtspfa
      361 slhlamnmac vkfgltpeea wagvtrhaar algrqashgq lapgfvanfa iwdaehpvem
      421 vyepgrsplw hrvvqgelq