AMIF_BACCR
ID AMIF_BACCR Reviewed; 332 AA.
AC P59701;
DT 30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2003, sequence version 1.
DT 25-MAY-2022, entry version 101.
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=BC_3939;
OS Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=226900;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC / NCTC 2599 / NRRL B-3711;
RX PubMed=12721630; DOI=10.1038/nature01582;
RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT anthracis.";
RL Nature 423:87-91(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; AE016877; AAP10859.1; -; Genomic_DNA.
DR RefSeq; NP_833658.1; NC_004722.1.
DR RefSeq; WP_000535802.1; NZ_CP034551.1.
DR PDB; 5G3O; X-ray; 2.15 A; A/B/C/D/E/F=1-332.
DR PDB; 5G3P; X-ray; 1.78 A; A/B/C/D/E/F=1-332.
DR PDBsum; 5G3O; -.
DR PDBsum; 5G3P; -.
DR AlphaFoldDB; P59701; -.
DR SMR; P59701; -.
DR STRING; 226900.BC_3939; -.
DR EnsemblBacteria; AAP10859; AAP10859; BC_3939.
DR KEGG; bce:BC3939; -.
DR PATRIC; fig|226900.8.peg.4063; -.
DR HOGENOM; CLU_071797_0_0_9; -.
DR OMA; RIWGCFS; -.
DR BRENDA; 3.5.1.49; 648.
DR Proteomes; UP000001417; 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..332
FT /note="Formamidase"
FT /id="PRO_0000204063"
FT DOMAIN 14..259
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 132
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01243"
FT ACT_SITE 165
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01243"
FT STRAND 13..19
FT /evidence="ECO:0007829|PDB:5G3P"
FT HELIX 29..49
FT /evidence="ECO:0007829|PDB:5G3P"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:5G3P"
FT TURN 60..64
FT /evidence="ECO:0007829|PDB:5G3P"
FT TURN 68..72
FT /evidence="ECO:0007829|PDB:5G3P"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:5G3P"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:5G3P"
FT HELIX 83..95
FT /evidence="ECO:0007829|PDB:5G3P"
FT STRAND 98..105
FT /evidence="ECO:0007829|PDB:5G3P"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:5G3P"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:5G3P"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:5G3P"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:5G3P"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:5G3O"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:5G3P"
FT STRAND 159..164
FT /evidence="ECO:0007829|PDB:5G3P"
FT HELIX 165..169
FT /evidence="ECO:0007829|PDB:5G3P"
FT HELIX 171..179
FT /evidence="ECO:0007829|PDB:5G3P"
FT STRAND 183..189
FT /evidence="ECO:0007829|PDB:5G3P"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:5G3P"
FT HELIX 196..209
FT /evidence="ECO:0007829|PDB:5G3P"
FT STRAND 213..218
FT /evidence="ECO:0007829|PDB:5G3P"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:5G3P"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:5G3P"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:5G3P"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:5G3P"
FT STRAND 252..257
FT /evidence="ECO:0007829|PDB:5G3P"
FT HELIX 259..268
FT /evidence="ECO:0007829|PDB:5G3P"
FT HELIX 274..277
FT /evidence="ECO:0007829|PDB:5G3P"
FT TURN 283..285
FT /evidence="ECO:0007829|PDB:5G3P"
FT HELIX 296..302
FT /evidence="ECO:0007829|PDB:5G3P"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:5G3P"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:5G3P"
SQ SEQUENCE 332 AA; 36767 MW; 5615B67F7DD95F37 CRC64;
MGSSGSMVKP ISGFLTALIQ YPVPVVESRA DIDKQIQQII KTIHSTKSGY PGLELIVFPE
YSTQGLNTKK WTTEEFLCTV PGPETDLFAE ACKESKVYGV FSIMEKNPDG GEPYNTAVII
DPQGEMILKY RKLNPWVPVE PWKAGDLGLP VCDGPGGSKL AVCICHDGMF PEVAREAAYK
GANVLIRISG YSTQVSEQWM LTNRSNAWQN LMYTLSVNLA GYDGVFYYFG EGQVCNFDGT
TLVQGHRNPW EIVTAEVYPE LADQARLGWG LENNIYNLGS RGYVATPGGV KENPYTFVKD
LAEGKYKVPW EDEIKVKDGS IYGYPVKKTI HS
