ID   YPQQ_PSEPH              Reviewed;         285 AA.
AC   P55176;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Hydrolase in pqqF 5'region;
DE            EC=3.5.-.-;
DE   AltName: Full=ORF2;
OS   Pseudomonas protegens (strain DSM 19095 / LMG 27888 / CFBP 6595 / CHA0).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1124983;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 19095 / LMG 27888 / CFBP 6595 / CHA0;
RX   PubMed=8526497; DOI=10.1128/aem.61.11.3856-3864.1995;
RA   Schnider U., Keel C., Defago G., Haas D.;
RT   "Tn5-directed cloning of pqq genes from Pseudomonas fluorescens CHA0:
RT   mutational inactivation of the genes results in overproduction of the
RT   antibiotic pyoluteorin.";
RL   Appl. Environ. Microbiol. 61:3856-3864(1995).
CC   -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC       NIT1/NIT2 family. {ECO:0000305}.
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DR   EMBL; X87299; CAA60729.1; -; Genomic_DNA.
DR   PIR; S58240; S58240.
DR   AlphaFoldDB; P55176; -.
DR   SMR; P55176; -.
DR   STRING; 1124983.PFLCHA0_c56230; -.
DR   PATRIC; fig|1124983.3.peg.5649; -.
DR   eggNOG; COG0388; Bacteria.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR   CDD; cd07576; R-amidase_like; 1.
DR   Gene3D; 3.60.110.10; -; 1.
DR   InterPro; IPR003010; C-N_Hydrolase.
DR   InterPro; IPR036526; C-N_Hydrolase_sf.
DR   InterPro; IPR044083; RamA-like.
DR   InterPro; IPR001110; UPF0012_CS.
DR   Pfam; PF00795; CN_hydrolase; 1.
DR   SUPFAM; SSF56317; SSF56317; 1.
DR   PROSITE; PS50263; CN_HYDROLASE; 1.
DR   PROSITE; PS01227; UPF0012; 1.
PE   3: Inferred from homology;
KW   Hydrolase.
FT   CHAIN           1..285
FT                   /note="Hydrolase in pqqF 5'region"
FT                   /id="PRO_0000213263"
FT   DOMAIN          22..258
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        60
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        131
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        165
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
SQ   SEQUENCE   285 AA;  31163 MW;  68B7C64F38CBDEC8 CRC64;
     MSYEPATAAT VAGLSVSGVK TMRVALYQCP PRPLDVAGNL QRLHQVAMEA TDADLLVLPE
     MFLSGYNIGL EAVGALAEAQ DGPSAQRIAA IAQAAGTAIL YGYPERSVDG QIYNAVQLID
     AQGQRLCNYR KTHLFGDLDH SMFSAGEDDF PLVELDGWKL GFLICYDIEF PENARRLALA
     GAELILVPTA NMIPYDFVAD VTIRARAFEN QCYVAYANYC GHEEQIRYCG QSSIAAPDGS
     RIALAGLDEA LIIGTLDRQL MGESRALNRY LSDRRPELYD DLSKR