ID   AMIF_HELAH              Reviewed;         334 AA.
AC   Q17WY3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=Hac_1079;
OS   Helicobacter acinonychis (strain Sheeba).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=382638;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sheeba;
RX   PubMed=16789826; DOI=10.1371/journal.pgen.0020120;
RA   Eppinger M., Baar C., Linz B., Raddatz G., Lanz C., Keller H., Morelli G.,
RA   Gressmann H., Achtman M., Schuster S.C.;
RT   "Who ate whom? Adaptive Helicobacter genomic changes that accompanied a
RT   host jump from early humans to large felines.";
RL   PLoS Genet. 2:1097-1110(2006).
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; AM260522; CAJ99843.1; -; Genomic_DNA.
DR   RefSeq; WP_011577952.1; NC_008229.1.
DR   AlphaFoldDB; Q17WY3; -.
DR   SMR; Q17WY3; -.
DR   STRING; 382638.Hac_1079; -.
DR   EnsemblBacteria; CAJ99843; CAJ99843; Hac_1079.
DR   KEGG; hac:Hac_1079; -.
DR   eggNOG; COG0388; Bacteria.
DR   HOGENOM; CLU_071797_0_0_7; -.
DR   OMA; RIWGCFS; -.
DR   OrthoDB; 1650683at2; -.
DR   BioCyc; HACI382638:HAC_RS04625-MON; -.
DR   Proteomes; UP000000775; 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_1000067060"
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;  37133 MW;  5CA77B85A2ED3CF3 CRC64;
     MGSIGSIGKP IEGFLVAAIQ FPVPIVNSKK DIENNVQSII RTLHATKAGY PGVELIIFPE
     YSTQGLNTAK WLSEEFLLDV GGKETEAYAQ ACKEAKVYGV FSIMERNPDP NKNPYNTAII
     INPKGEIILH YRKLFPWNPI EPWYPGDKGM PVCDGPGGSK LAVCICHDGM IPELAREAAY
     KGCNVYIRIS GYSTQVNDQW ILTNRSNAWH NLMYTVSVNL AGYDNVFYYF GEGQICNFDG
     TTLVQGHRNP WEIVTGEIYP KMADNARLSW GLENNIYNLG HRGYVAKPGG EPDAGLTYIK
     DLAASKYKLP WEDHMQIKDG SIYGYPTSGG RFGK