ID   AMIF_BACC4              Reviewed;         332 AA.
AC   B7H6S5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 64.
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=BCB4264_A4041;
OS   Bacillus cereus (strain B4264).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405532;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4264;
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 B4264.";
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; CP001176; ACK59209.1; -; Genomic_DNA.
DR   RefSeq; WP_000535802.1; NZ_VEHB01000002.1.
DR   AlphaFoldDB; B7H6S5; -.
DR   SMR; B7H6S5; -.
DR   EnsemblBacteria; ACK59209; ACK59209; BCB4264_A4041.
DR   KEGG; bcb:BCB4264_A4041; -.
DR   HOGENOM; CLU_071797_0_0_9; -.
DR   OMA; RIWGCFS; -.
DR   Proteomes; UP000007096; 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_1000139812"
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;  36767 MW;  5615B67F7DD95F37 CRC64;
     MGSSGSMVKP ISGFLTALIQ YPVPVVESRA DIDKQIQQII KTIHSTKSGY PGLELIVFPE
     YSTQGLNTKK WTTEEFLCTV PGPETDLFAE ACKESKVYGV FSIMEKNPDG GEPYNTAVII
     DPQGEMILKY RKLNPWVPVE PWKAGDLGLP VCDGPGGSKL AVCICHDGMF PEVAREAAYK
     GANVLIRISG YSTQVSEQWM LTNRSNAWQN LMYTLSVNLA GYDGVFYYFG EGQVCNFDGT
     TLVQGHRNPW EIVTAEVYPE LADQARLGWG LENNIYNLGS RGYVATPGGV KENPYTFVKD
     LAEGKYKVPW EDEIKVKDGS IYGYPVKKTI HS