AMIF_AGRVS
ID AMIF_AGRVS Reviewed; 338 AA.
AC B9K1J4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 62.
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=Avi_5655;
OS Agrobacterium vitis (strain S4 / ATCC BAA-846) (Rhizobium vitis (strain
OS S4)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium.
OX NCBI_TaxID=311402;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S4 / ATCC BAA-846;
RX PubMed=19251847; DOI=10.1128/jb.01779-08;
RA Slater S.C., Goldman B.S., Goodner B., Setubal J.C., Farrand S.K.,
RA Nester E.W., Burr T.J., Banta L., Dickerman A.W., Paulsen I., Otten L.,
RA Suen G., Welch R., Almeida N.F., Arnold F., Burton O.T., Du Z., Ewing A.,
RA Godsy E., Heisel S., Houmiel K.L., Jhaveri J., Lu J., Miller N.M.,
RA Norton S., Chen Q., Phoolcharoen W., Ohlin V., Ondrusek D., Pride N.,
RA Stricklin S.L., Sun J., Wheeler C., Wilson L., Zhu H., Wood D.W.;
RT "Genome sequences of three Agrobacterium biovars help elucidate the
RT evolution of multichromosome genomes in bacteria.";
RL J. Bacteriol. 191:2501-2511(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; CP000634; ACM38742.1; -; Genomic_DNA.
DR RefSeq; WP_012653984.1; NC_011988.1.
DR AlphaFoldDB; B9K1J4; -.
DR SMR; B9K1J4; -.
DR STRING; 311402.Avi_5655; -.
DR EnsemblBacteria; ACM38742; ACM38742; Avi_5655.
DR KEGG; avi:Avi_5655; -.
DR eggNOG; COG0388; Bacteria.
DR HOGENOM; CLU_071797_0_0_5; -.
DR OMA; RIWGCFS; -.
DR OrthoDB; 1650683at2; -.
DR Proteomes; UP000001596; Chromosome 2.
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_1000165035"
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 338 AA; 36924 MW; 8E800D6894FC1FD3 CRC64;
MNGLGGLNKS EHGVGIGLVQ LQLPVTVTPQ DLARQTQVIV DLVAKARRNQ PGMDLVVFPE
YALHGLSMDI NPDIMCRMDG PEVAAFKAAC KQNRIWGCFS IMEYNPGGMP YNSGIIIDDT
GALKLYYRKM HPWVPVEPWE PGDLGIPVID GPKGAKLALI ICHDGMFPEM ARECAYKGAE
IMIRTAGYTA PIRESWRFTN QSNAFCNLMV TANVCMCGSD GTFDSMGEGM ICNFDGSIIA
HGTSGRVNEI ITAEVRPDLV REARLGWGVE NNIYQLGHRG YVAVAGGAQD APYTYMHDLA
AGRYRLPWEV EVKITDGTAC GFEKPTRLYG KPAKSAAE