AMIF_PHOLL
ID AMIF_PHOLL Reviewed; 338 AA.
AC Q7N278;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=plu3213;
OS Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS TT01).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus.
OX NCBI_TaxID=243265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15139 / CIP 105565 / TT01;
RX PubMed=14528314; DOI=10.1038/nbt886;
RA Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA Glaser P., Boemare N., Danchin A., Kunst F.;
RT "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT luminescens.";
RL Nat. Biotechnol. 21:1307-1313(2003).
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; BX571869; CAE15587.1; -; Genomic_DNA.
DR RefSeq; WP_011147417.1; NC_005126.1.
DR AlphaFoldDB; Q7N278; -.
DR SMR; Q7N278; -.
DR STRING; 243265.plu3213; -.
DR EnsemblBacteria; CAE15587; CAE15587; plu3213.
DR GeneID; 24169969; -.
DR KEGG; plu:plu3213; -.
DR eggNOG; COG0388; Bacteria.
DR HOGENOM; CLU_071797_0_0_6; -.
DR OMA; RIWGCFS; -.
DR OrthoDB; 1650683at2; -.
DR BioCyc; PLUM243265:PLU_RS15995-MON; -.
DR Proteomes; UP000002514; 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..338
FT /note="Formamidase"
FT /id="PRO_1000165040"
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 338 AA; 38509 MW; 1906BA5F84F92611 CRC64;
MGSTGSVSAW DEALLIAAIQ YPVPIIRGPE DIQVQVQQIC KTMDSTKAGY PDLDFIVFPE
YSAQGLNTKI WTYDEMLLSL DSPEIDCFRR ACIRNDVWGV FSIMERNEDP SQIPYNTAII
INSNGEIVLH YRKLQPWVPI EPWMPGNLGM PVCEGPKGAK LAVCICHDGM FPELAREAAY
KGCNVFIRIS GYSTQVNDQW IWTNRTNAWQ NLMYTVSVNL AGYDEVFYYF GEGTICNYDG
NIIQQGQRNP WEIVTAELFP RLADKARENW ALENSIFNLG CRGYVGKPGG ERANYLTWVR
DLANGEYKLP WDENIRIRDG WKYYPEGVKL GPLPKIDE
