AMIF_BRADU
ID AMIF_BRADU Reviewed; 337 AA.
AC Q89H51;
DT 30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2003, sequence version 1.
DT 25-MAY-2022, entry version 91.
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=blr6144;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
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; BA000040; BAC51409.1; -; Genomic_DNA.
DR RefSeq; NP_772784.1; NC_004463.1.
DR RefSeq; WP_011088885.1; NZ_CP011360.1.
DR AlphaFoldDB; Q89H51; -.
DR SMR; Q89H51; -.
DR STRING; 224911.27354422; -.
DR EnsemblBacteria; BAC51409; BAC51409; BAC51409.
DR GeneID; 64025905; -.
DR KEGG; bja:blr6144; -.
DR PATRIC; fig|224911.44.peg.6107; -.
DR eggNOG; COG0388; Bacteria.
DR HOGENOM; CLU_071797_0_0_5; -.
DR InParanoid; Q89H51; -.
DR OMA; RIWGCFS; -.
DR PhylomeDB; Q89H51; -.
DR Proteomes; UP000002526; Chromosome.
DR GO; GO:0004328; F:formamidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..337
FT /note="Formamidase"
FT /id="PRO_0000204064"
FT DOMAIN 14..257
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 129
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01243"
FT ACT_SITE 162
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01243"
SQ SEQUENCE 337 AA; 37343 MW; AC3C8BEE0E53619D CRC64;
MNGLGGLNKS PEGVVIGLVQ LQLPNVVTRA DLARQTERIV WMVGKARRNL STMDLVVFPE
YSLHGLSMDT NPEIMCRLDG PEVTAFKKAC VDNRIWGCFS IMEFNPHGNP YNSGLIIDDH
GEIKLYYRKL HPWIPVEPWE PGDIGIPVIE GPKGARIALI ICHDGMFPEM ARECAYKGAE
IMIRTAGYTA PIREAWRFTN QANSFQNLMV TANVCMCGSD GSFDSMGEGM IVNFDGAVLA
HGTTGRADEI ITAEVRPDLV REARINWGVE NNIYQLWHRG YVAVKGGAMD CPYTFMQDMV
AGTFRLPWED QVKVTDGSSC GFPAPTRMYG KTAKAAE
