AMIF_PSESM
ID AMIF_PSESM Reviewed; 338 AA.
AC Q887D9;
DT 30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2003, sequence version 1.
DT 25-MAY-2022, entry version 95.
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}; Synonyms=amiE;
GN OrderedLocusNames=PSPTO_1357;
OS Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=223283;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-871 / DC3000;
RX PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA Collmer A.;
RT "The complete genome sequence of the Arabidopsis and tomato pathogen
RT Pseudomonas syringae pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(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; AE016853; AAO54879.1; -; Genomic_DNA.
DR RefSeq; NP_791184.1; NC_004578.1.
DR RefSeq; WP_011103524.1; NC_004578.1.
DR AlphaFoldDB; Q887D9; -.
DR SMR; Q887D9; -.
DR STRING; 223283.PSPTO_1357; -.
DR EnsemblBacteria; AAO54879; AAO54879; PSPTO_1357.
DR GeneID; 1182993; -.
DR KEGG; pst:PSPTO_1357; -.
DR PATRIC; fig|223283.9.peg.1379; -.
DR eggNOG; COG0388; Bacteria.
DR HOGENOM; CLU_071797_0_0_6; -.
DR OMA; RIWGCFS; -.
DR OrthoDB; 1650683at2; -.
DR PhylomeDB; Q887D9; -.
DR Proteomes; UP000002515; Chromosome.
DR GO; GO:0004040; F:amidase activity; ISS:JCVI.
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_0000204067"
FT DOMAIN 15..257
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 61
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01243"
FT ACT_SITE 130
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01243"
FT ACT_SITE 163
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01243"
SQ SEQUENCE 338 AA; 37253 MW; 1B47EF8A07392DD1 CRC64;
MASGLGGLNK SPNGVVIGLA QLALPDPHTR EALWAQTQKV VGMVAKARRS NPGMDLIVFP
EYSLHGLSMS TAPEIMCSLD GPEVVALREA CKEHRIWGCF SIMEANPQGN PFNSSLIVDD
LGEIRLYYRK LHPWVPVEPW EPGDLGIPVC DGPRGSTLAL IICHDGMFPE MARECAYKGA
DIMLRTAGYT APIRHSWKIT NQSNAFTNLM QTASVCMCGS DGTFDSMGEA MFVDFDGTIM
AEGGGRADEI VCCELRPDLV REARVHWGVE NNIYQFGHRG YVAVKGGARD CPYTYMRDLT
AGQYRLPWEN DVVHTDGRSC GFATPEREFK PTPSSWKE