ID   AMIF_BACCQ              Reviewed;         332 AA.
AC   B9IW18;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 60.
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=BCQ_3727;
OS   Bacillus cereus (strain Q1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=361100;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Q1;
RX   PubMed=19060151; DOI=10.1128/jb.01629-08;
RA   Xiong Z., Jiang Y., Qi D., Lu H., Yang F., Yang J., Chen L., Sun L., Xu X.,
RA   Xue Y., Zhu Y., Jin Q.;
RT   "Complete genome sequence of the extremophilic Bacillus cereus strain Q1
RT   with industrial applications.";
RL   J. Bacteriol. 191:1120-1121(2009).
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; CP000227; ACM14155.1; -; Genomic_DNA.
DR   RefSeq; WP_000535784.1; NC_011969.1.
DR   AlphaFoldDB; B9IW18; -.
DR   SMR; B9IW18; -.
DR   EnsemblBacteria; ACM14155; ACM14155; BCQ_3727.
DR   KEGG; bcq:BCQ_3727; -.
DR   HOGENOM; CLU_071797_0_0_9; -.
DR   OMA; RIWGCFS; -.
DR   Proteomes; UP000000441; 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_1000165039"
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;  36778 MW;  CD10A6BADD05DC5A CRC64;
     MGSSGSMVKP ISGFLAALIQ YPVPVVESRA DIDKQIKQII KTIHSTKAGY PGLELIVFPE
     YSTQGLNTKK WTTEEFLCTV PGPETDLFAE ACKESEVYGV FSLMERNPDG GEPYNTAIII
     DPQGEMILKY RKLNPWVPVE PWKAGDLGLP VCDGPGGSKL AVCICHDGMF PEVAREAAYK
     GANVLIRISG YSTQVSEQWM LTNRSNAWQN LMYTLSVNLA GYDGVFYYFG EGQVCNFDGT
     TLVQGHRNPW EIVTAEVYPE LADQARLGWG LENNIYNLGS RGYVATPGGV KENPYTFVKD
     LAEGKYKVPW EDEIKVKDGT IYGYPVKKTI HS