ID AMIF_BACAC Reviewed; 332 AA.
AC C3LI05;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 61.
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=BAMEG_4192;
OS Bacillus anthracis (strain CDC 684 / NRRL 3495).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=568206;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 684 / NRRL 3495;
RA Dodson R.J., Munk A.C., Brettin T., Bruce D., Detter C., Tapia R., Han C.,
RA Sutton G., Sims D.;
RT "Genome sequence of Bacillus anthracis str. CDC 684.";
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; CP001215; ACP14530.1; -; Genomic_DNA.
DR RefSeq; WP_000535791.1; NC_012581.1.
DR AlphaFoldDB; C3LI05; -.
DR SMR; C3LI05; -.
DR GeneID; 45023826; -.
DR KEGG; bah:BAMEG_4192; -.
DR HOGENOM; CLU_071797_0_0_9; -.
DR GO; GO:0004328; F:formamidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR CDD; cd07565; aliphatic_amidase; 1.
DR Gene3D; 3.60.110.10; Carbon-nitrogen hydrolase; 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 PANTHER; PTHR43674:SF14; ALIPHATIC AMIDASE; 1.
DR PANTHER; PTHR43674; NITRILASE C965.09-RELATED; 1.
DR Pfam; PF00795; CN_hydrolase; 1.
DR SUPFAM; SSF56317; Carbon-nitrogen hydrolase; 1.
DR PROSITE; PS50263; CN_HYDROLASE; 1.
PE 3: Inferred from homology;
KW Hydrolase.
FT CHAIN 1..332
FT /note="Formamidase"
FT /id="PRO_1000165037"
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; 36808 MW; B5658028DC96983B CRC64;
MGSSGSMVKP ISGFLTALIQ YPVPVVESRA DIDKQIKQII KTIHSTKAGY PGLELIVFPE
YSTQGLNTKK WTTEEFLCTV PGPETDLFAE ACKESEVYGV FSIMERNPDG GEPYNTAIII
DPQGEMILKY RKLNPWVPVE PWKAGDLGLP VCDGPGGSKL AVCICHDGMF PEVAREAAYK
GANVLIRISG YSTQVSEQWM LTNRSNAWQN LMYTLSVNLA GYDGVFYYFG EGQVCNFDGT
TLVQGHRNPW EIVTAEVYPE LADQARLGWG LENNIYNLGS RGYVATPGGV KENPYTFVKD
LAEGKYKVPW EDEIKVKDGT IYGYPVKKTI HS
//
