ID   AMIF_DESVV              Reviewed;         334 AA.
AC   A1VEP0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 65.
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=Dvul_1889;
OS   Desulfovibrio vulgaris subsp. vulgaris (strain DP4).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=391774;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DP4;
RX   PubMed=19737303; DOI=10.1111/j.1462-2920.2009.01946.x;
RA   Walker C.B., Stolyar S., Chivian D., Pinel N., Gabster J.A., Dehal P.S.,
RA   He Z., Yang Z.K., Yen H.C., Zhou J., Wall J.D., Hazen T.C., Arkin A.P.,
RA   Stahl D.A.;
RT   "Contribution of mobile genetic elements to Desulfovibrio vulgaris genome
RT   plasticity.";
RL   Environ. Microbiol. 11:2244-2252(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; CP000527; ABM28906.1; -; Genomic_DNA.
DR   RefSeq; WP_010938461.1; NC_008751.1.
DR   AlphaFoldDB; A1VEP0; -.
DR   SMR; A1VEP0; -.
DR   EnsemblBacteria; ABM28906; ABM28906; Dvul_1889.
DR   KEGG; dvl:Dvul_1889; -.
DR   HOGENOM; CLU_071797_0_0_7; -.
DR   OMA; RIWGCFS; -.
DR   Proteomes; UP000009173; 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_1000067059"
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;  37483 MW;  DE21B989EA00C5A6 CRC64;
     MGSIGSMNKP SEGMLMGLVQ YPVPIVNSRR DIEASVDRIC AATAATKAGY PGMDLIVWPE
     YSTQGLNTKK WVTEEFLMDV EEPLFQRYAQ TCKENDVWGV FSIMERNPNK NQMPYNTAVI
     FNNKGELALK YRKLNPWVPI EPWMPGDLGQ PVCDGPGGSK LSLCICHDGM FPEQAREAAY
     KGCNVYIRIS GYSTQVNEQW ILTNRSNAWH NLMYTAAVNL AGYDGVFYYF GEGQVCNFDG
     TTLVQGHRNP WEIVTAEVFP KMADQARTDW GLENNIFNVG TRGYVAHPGG VKDCPYTWVK
     DFAAGKYHLP WEDKIKIKDG SIYGYPTTGG RFGL