ID   AMIF_HELPS              Reviewed;         334 AA.
AC   B2UV01;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 59.
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=HPSH_06405;
OS   Helicobacter pylori (strain Shi470).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=512562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Shi470;
RA   Kersulyte D., Kalia A., Gilman R.H., Berg D.E.;
RT   "Genome sequence of Helicobacter pylori from the remote Amazon: traces of
RT   Asian ancestry of the first Americans.";
RL   Submitted (MAY-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; CP001072; ACD48683.1; -; Genomic_DNA.
DR   RefSeq; WP_000534777.1; NC_010698.2.
DR   AlphaFoldDB; B2UV01; -.
DR   SMR; B2UV01; -.
DR   KEGG; hps:HPSH_06405; -.
DR   HOGENOM; CLU_071797_0_0_7; -.
DR   OMA; RIWGCFS; -.
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_1000139815"
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;  37276 MW;  B6801447B0034A8A CRC64;
     MGSIGSMGKP IEGFLVAAIQ FPVPIVNSRK DIDHNIESII RTLHATKAGY PGVELIIFPE
     YSTQGLNTAK WLSEEFLLDV PGKETELYAK ACKEAKVYGV FSIMERNPDS NKNPYNTAII
     IDPQGKIILK YRKLFPWNPI EPWYPGDLGM PVCEGPGGSK LAVCICHDGM IPELAREAAY
     KGCNVYIRIS GYSTQVNDQW ILTNRSNAWH NLMYTVSVNL AGYDNVFYYF GEGQICNFDG
     TTLVQGHRNP WEIVTGEIYP KMADNARLSW GLENNIYNLG HRGYVAKPGG EHDAGLTYIK
     DLAAGKYKLP WEDHMKIKDG SVYGYPTTGG RFGK