ID   AMIF_HELP2              Reviewed;         334 AA.
AC   B6JN78;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   25-MAY-2022, entry version 55.
DE   RecName: Full=Formamidase {ECO:0000255|HAMAP-Rule:MF_01243};
DE            EC=3.5.1.49 {ECO:0000255|HAMAP-Rule:MF_01243};
DE   AltName: Full=Formamide amidohydrolase {ECO:0000255|HAMAP-Rule:MF_01243};
GN   Name=amiF {ECO:0000255|HAMAP-Rule:MF_01243}; OrderedLocusNames=HPP12_1204;
OS   Helicobacter pylori (strain P12).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=570508;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P12;
RA   Fischer W., Windhager L., Karnholz A., Zeiller M., Zimmer R., Haas R.;
RT   "The complete genome sequence of Helicobacter pylori strain P12.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Is an aliphatic amidase with a restricted substrate
CC       specificity, as it only hydrolyzes formamide. {ECO:0000255|HAMAP-
CC       Rule:MF_01243}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=formamide + H2O = formate + NH4(+); Xref=Rhea:RHEA:21948,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15740, ChEBI:CHEBI:16397,
CC         ChEBI:CHEBI:28938; EC=3.5.1.49; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01243};
CC   -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC       Aliphatic amidase family. {ECO:0000255|HAMAP-Rule:MF_01243}.
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DR   EMBL; CP001217; ACJ08356.1; -; Genomic_DNA.
DR   RefSeq; WP_000534759.1; NC_011498.1.
DR   AlphaFoldDB; B6JN78; -.
DR   SMR; B6JN78; -.
DR   EnsemblBacteria; ACJ08356; ACJ08356; HPP12_1204.
DR   KEGG; hpp:HPP12_1204; -.
DR   HOGENOM; CLU_071797_0_0_7; -.
DR   OMA; RIWGCFS; -.
DR   OrthoDB; 1650683at2; -.
DR   Proteomes; UP000008198; Chromosome.
DR   GO; GO:0004328; F:formamidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR   Gene3D; 3.60.110.10; -; 1.
DR   HAMAP; MF_01243; Formamidase; 1.
DR   InterPro; IPR003010; C-N_Hydrolase.
DR   InterPro; IPR036526; C-N_Hydrolase_sf.
DR   InterPro; IPR022843; Formamidase.
DR   Pfam; PF00795; CN_hydrolase; 1.
DR   SUPFAM; SSF56317; SSF56317; 1.
DR   PROSITE; PS50263; CN_HYDROLASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase.
FT   CHAIN           1..334
FT                   /note="Formamidase"
FT                   /id="PRO_1000139813"
FT   DOMAIN          14..260
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        60
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01243"
FT   ACT_SITE        133
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01243"
FT   ACT_SITE        166
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01243"
SQ   SEQUENCE   334 AA;  37247 MW;  106014405C8756F9 CRC64;
     MGSIGSMGKP IEGFLVAAIQ FPVPIVNSRK DIDHNIESII RTLHATKAGY PGVELIIFPE
     YSTQGLNTAK WLSEEFLLDV PGKETEAYAQ ACKEAKVYGV FSIMERNPDS NKNPYNTAII
     IDPQGKIILK YRKLFPWNPI EPWYPGDLGM PVCEGPGGSK LAVCICHDGM IPELAREAAY
     KGCNVYIRIS GYSTQVNDQW ILTNRSNAWH NLMYTVSVNL AGYDNVFYYF GEGQICNFDG
     TTLVQGHRNP WEIVTGEIYP KMADNARLSW GLENNIYNLG HRGYVAKPGG EHDAGLTYIK
     DLAAGKYKLP WEDHMKIKDG SIYGYPTTGG RFGK