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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
 
 
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