AMIF_BRASO
ID AMIF_BRASO Reviewed; 337 AA.
AC A4Z3G9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 66.
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=BRADO7112;
OS Bradyrhizobium sp. (strain ORS 278).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium; unclassified Bradyrhizobium.
OX NCBI_TaxID=114615;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ORS 278;
RX PubMed=17540897; DOI=10.1126/science.1139548;
RA Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.-C.,
RA Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L.,
RA Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., Rouy Z.,
RA Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.-S., Saunders E.,
RA Bruce D., Richardson P., Normand P., Dreyfus B., Pignol D., Stacey G.,
RA Emerich D., Vermeglio A., Medigue C., Sadowsky M.;
RT "Legumes symbioses: absence of nod genes in photosynthetic bradyrhizobia.";
RL Science 316:1307-1312(2007).
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; CU234118; CAL80695.1; -; Genomic_DNA.
DR RefSeq; WP_012030555.1; NC_009445.1.
DR AlphaFoldDB; A4Z3G9; -.
DR SMR; A4Z3G9; -.
DR STRING; 114615.BRADO7112; -.
DR EnsemblBacteria; CAL80695; CAL80695; BRADO7112.
DR KEGG; bra:BRADO7112; -.
DR eggNOG; COG0388; Bacteria.
DR HOGENOM; CLU_071797_0_0_5; -.
DR OMA; RIWGCFS; -.
DR OrthoDB; 1650683at2; -.
DR BioCyc; BSP114615:BRADO_RS33005-MON; -.
DR Proteomes; UP000001994; 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; Reference proteome.
FT CHAIN 1..337
FT /note="Formamidase"
FT /id="PRO_1000067057"
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; 37205 MW; F2D0256951FC934A CRC64;
MNGLGGLNKS EHGVVIGLVQ LQLPVVVTKE DLAKQTEKIV WMVGKARRNL GTMDLVVFPE
YSLHGLSMDT NPEIMCRLDG PEVAAFKQAC IDNKIWGCFS IMEYNPDGNP YNSGLIIDSN
GEIKLYYRKL HPWIPVEPWE PGDLGIPVIE GPRGAKIALI ICHDGMFPEM ARECAYKGAE
IMIRTAGYTA PIRDSWRFTN QANAFQNLMV TANVCMCGSD GSFDSMGEGM IVNFDGSILA
HGTTGRADEI ITAEVRPDLV REARIGWGVE NNIYQLWHRG YVAVKGGAMD CPYTFMHDMV
AGTYRLPWED QVKITDGTSC GFPAPTRVFG KMAKAAE
