AMIF_DESVH
ID AMIF_DESVH Reviewed; 334 AA.
AC Q72CW9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=DVU_1164;
OS Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS B-1760 / Hildenborough).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough;
RX PubMed=15077118; DOI=10.1038/nbt959;
RA Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M.,
RA Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J.,
RA Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G.,
RA Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., Feldblyum T.V.,
RA Wall J.D., Voordouw G., Fraser C.M.;
RT "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT Desulfovibrio vulgaris Hildenborough.";
RL Nat. Biotechnol. 22:554-559(2004).
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; AE017285; AAS95642.1; -; Genomic_DNA.
DR RefSeq; WP_010938461.1; NZ_CABHLV010000001.1.
DR RefSeq; YP_010383.1; NC_002937.3.
DR AlphaFoldDB; Q72CW9; -.
DR SMR; Q72CW9; -.
DR STRING; 882.DVU_1164; -.
DR PaxDb; Q72CW9; -.
DR EnsemblBacteria; AAS95642; AAS95642; DVU_1164.
DR KEGG; dvu:DVU_1164; -.
DR PATRIC; fig|882.5.peg.1093; -.
DR eggNOG; COG0388; Bacteria.
DR HOGENOM; CLU_071797_0_0_7; -.
DR OMA; RIWGCFS; -.
DR PhylomeDB; Q72CW9; -.
DR Proteomes; UP000002194; 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..334
FT /note="Formamidase"
FT /id="PRO_1000067058"
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 334 AA; 37483 MW; DE21B989EA00C5A6 CRC64;
MGSIGSMNKP SEGMLMGLVQ YPVPIVNSRR DIEASVDRIC AATAATKAGY PGMDLIVWPE
YSTQGLNTKK WVTEEFLMDV EEPLFQRYAQ TCKENDVWGV FSIMERNPNK NQMPYNTAVI
FNNKGELALK YRKLNPWVPI EPWMPGDLGQ PVCDGPGGSK LSLCICHDGM FPEQAREAAY
KGCNVYIRIS GYSTQVNEQW ILTNRSNAWH NLMYTAAVNL AGYDGVFYYF GEGQVCNFDG
TTLVQGHRNP WEIVTAEVFP KMADQARTDW GLENNIFNVG TRGYVAHPGG VKDCPYTWVK
DFAAGKYHLP WEDKIKIKDG SIYGYPTTGG RFGL