ID   AMIF_BACC2              Reviewed;         332 AA.
AC   B7IVH6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-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};
GN   OrderedLocusNames=BCG9842_B1198;
OS   Bacillus cereus (strain G9842).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405531;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G9842;
RA   Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA   Ravel J., Sutton G.;
RT   "Genome sequence of Bacillus cereus G9842.";
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; CP001186; ACK93411.1; -; Genomic_DNA.
DR   RefSeq; WP_000535809.1; NC_011772.1.
DR   AlphaFoldDB; B7IVH6; -.
DR   SMR; B7IVH6; -.
DR   EnsemblBacteria; ACK93411; ACK93411; BCG9842_B1198.
DR   KEGG; bcg:BCG9842_B1198; -.
DR   HOGENOM; CLU_071797_0_0_9; -.
DR   OMA; RIWGCFS; -.
DR   Proteomes; UP000006744; 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..332
FT                   /note="Formamidase"
FT                   /id="PRO_1000139811"
FT   DOMAIN          14..259
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        132
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01243"
FT   ACT_SITE        165
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01243"
SQ   SEQUENCE   332 AA;  36707 MW;  C7367A088A6670E9 CRC64;
     MGSSGSMVKP ISGFLTALIQ YPVPVVESRA DIDKQIQQII KTIHSTKSGY PGLELIVFPE
     YSTQGLNTKK WTTEEFLCTV PGPETDLFAE ACKESKVYGV FSIMEKNPGG GEPYNTAVII
     DPQGEMILKY RKLNPWVPVE PWKAGDLGLP VCVGPGGSKL AVCICHDGMF PEVAREAAYK
     GANVLIRISG YSTQVSEQWM LTNRSNAWQN LMYTLSVNLA GYDGVFYYFG EGQVCNFDGT
     TLVQGHRNPW EIVTAEVYPE LADQARLGWG LENNIYNLGS RGYVATPGGV KENPYTFIKD
     LAEGKYKVPW EDEIKVKDGS IYGYPVKKTI HS