AMIF_HELPY
ID AMIF_HELPY Reviewed; 334 AA.
AC O25836;
DT 30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Formamidase;
DE EC=3.5.1.49;
DE AltName: Full=Formamide amidohydrolase;
GN Name=amiF; OrderedLocusNames=HP_1238;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, AND MUTAGENESIS OF CYS-166 AND ASP-168.
RX PubMed=11359566; DOI=10.1046/j.1365-2958.2001.02400.x;
RA Skouloubris S., Labigne A., De Reuse H.;
RT "The AmiE aliphatic amidase and AmiF formamidase of Helicobacter pylori:
RT natural evolution of two enzyme paralogues.";
RL Mol. Microbiol. 40:596-609(2001).
RN [3]
RP ACTIVITY REGULATION, AND INDUCTION.
RX PubMed=12499381; DOI=10.1074/jbc.m207542200;
RA van Vliet A.H.M., Stoof J., Poppelaars S.W., Bereswill S., Homuth G.,
RA Kist M., Kuipers E.J., Kusters J.G.;
RT "Differential regulation of amidase- and formamidase-mediated ammonia
RT production by the Helicobacter pylori fur repressor.";
RL J. Biol. Chem. 278:9052-9057(2003).
CC -!- FUNCTION: Is an aliphatic amidase with a restricted substrate
CC specificity, as it only hydrolyzes formamide. Probably involved in the
CC nitrogen metabolism of H.pylori. {ECO:0000269|PubMed:11359566}.
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;
CC Evidence={ECO:0000269|PubMed:11359566};
CC -!- ACTIVITY REGULATION: Inhibited by iodoacetate. Appears to be regulated
CC by the fur protein, but this effect is not mediated at the
CC transcriptional level. {ECO:0000269|PubMed:11359566,
CC ECO:0000269|PubMed:12499381}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6. {ECO:0000269|PubMed:11359566};
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius.
CC {ECO:0000269|PubMed:11359566};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:11359566}.
CC -!- INDUCTION: Unlike the other amidase AmiE, expression of amiF is not
CC repressed by iron. {ECO:0000269|PubMed:12499381}.
CC -!- MISCELLANEOUS: Asp-168 is probably not involved in the catalytic
CC mechanism, but is probably involved instead in maintenance of the
CC structural integrity of the amidase. {ECO:0000305|PubMed:11359566}.
CC -!- MISCELLANEOUS: Expression of the amiF gene is stimulated in a mutant
CC deficient in arginase activity, suggesting that production of this
CC enzyme is regulated to maintain intracellular nitrogen balance in
CC H.pylori.
CC -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC Aliphatic amidase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000511; AAD08283.1; -; Genomic_DNA.
DR PIR; F64674; F64674.
DR RefSeq; NP_208030.1; NC_000915.1.
DR RefSeq; WP_000534771.1; NC_018939.1.
DR PDB; 2DYU; X-ray; 1.75 A; A/B=1-334.
DR PDB; 2DYV; X-ray; 2.00 A; A/B=1-334.
DR PDB; 2E2K; X-ray; 2.50 A; A/B/C/D/E/F=1-334.
DR PDB; 2E2L; X-ray; 2.29 A; A/B/C/D/E/F=1-334.
DR PDBsum; 2DYU; -.
DR PDBsum; 2DYV; -.
DR PDBsum; 2E2K; -.
DR PDBsum; 2E2L; -.
DR AlphaFoldDB; O25836; -.
DR SMR; O25836; -.
DR IntAct; O25836; 3.
DR MINT; O25836; -.
DR STRING; 85962.C694_06390; -.
DR PaxDb; O25836; -.
DR EnsemblBacteria; AAD08283; AAD08283; HP_1238.
DR KEGG; hpy:HP_1238; -.
DR PATRIC; fig|85962.47.peg.1326; -.
DR eggNOG; COG0388; Bacteria.
DR OMA; RIWGCFS; -.
DR PhylomeDB; O25836; -.
DR BRENDA; 3.5.1.49; 2604.
DR EvolutionaryTrace; O25836; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0004328; F:formamidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Reference proteome.
FT CHAIN 1..334
FT /note="Formamidase"
FT /id="PRO_0000204065"
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:0000250"
FT ACT_SITE 133
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 166
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT MUTAGEN 166
FT /note="C->S,A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11359566"
FT MUTAGEN 168
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11359566"
FT STRAND 14..19
FT /evidence="ECO:0007829|PDB:2DYU"
FT HELIX 29..49
FT /evidence="ECO:0007829|PDB:2DYU"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:2DYU"
FT TURN 60..64
FT /evidence="ECO:0007829|PDB:2DYU"
FT TURN 68..72
FT /evidence="ECO:0007829|PDB:2DYU"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:2DYU"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:2DYU"
FT HELIX 83..95
FT /evidence="ECO:0007829|PDB:2DYU"
FT STRAND 98..105
FT /evidence="ECO:0007829|PDB:2DYU"
FT STRAND 115..121
FT /evidence="ECO:0007829|PDB:2DYU"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:2DYU"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:2DYU"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:2DYU"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:2DYU"
FT HELIX 166..170
FT /evidence="ECO:0007829|PDB:2DYU"
FT HELIX 172..180
FT /evidence="ECO:0007829|PDB:2DYU"
FT STRAND 184..192
FT /evidence="ECO:0007829|PDB:2DYU"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:2E2L"
FT HELIX 197..211
FT /evidence="ECO:0007829|PDB:2DYU"
FT STRAND 214..219
FT /evidence="ECO:0007829|PDB:2DYU"
FT STRAND 221..226
FT /evidence="ECO:0007829|PDB:2DYU"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:2DYU"
FT STRAND 242..245
FT /evidence="ECO:0007829|PDB:2DYU"
FT STRAND 253..258
FT /evidence="ECO:0007829|PDB:2DYU"
FT HELIX 260..269
FT /evidence="ECO:0007829|PDB:2DYU"
FT HELIX 275..278
FT /evidence="ECO:0007829|PDB:2DYU"
FT TURN 284..288
FT /evidence="ECO:0007829|PDB:2DYU"
FT HELIX 297..303
FT /evidence="ECO:0007829|PDB:2DYU"
FT HELIX 312..314
FT /evidence="ECO:0007829|PDB:2DYU"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:2DYU"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:2DYU"
SQ SEQUENCE 334 AA; 37291 MW; B2845E0902A40420 CRC64;
MGSIGSMGKP IEGFLVAAIQ FPVPIVNSRK DIDHNIESII RTLHATKAGY PGVELIIFPE
YSTQGLNTAK WLSEEFLLDV PGKETELYAK ACKEAKVYGV FSIMERNPDS NKNPYNTAII
IDPQGEIILK YRKLFPWNPI EPWYPGDLGM PVCEGPGGSK LAVCICHDGM IPELAREAAY
KGCNVYIRIS GYSTQVNDQW ILTNRSNAWH NLMYTVSVNL AGYDNVFYYF GEGQICNFDG
TTLVQGHRNP WEIVTGEIYP KMADNARLSW GLENNIYNLG HRGYVAKPGG EHDAGLTYIK
DLAAGKYKLP WEDHMKIKDG SIYGYPTTGG RFGK
