NIT_RHIFH
ID NIT_RHIFH Reviewed; 308 AA.
AC G9AIU0; A0A0P1DJR8;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2012, sequence version 1.
DT 25-MAY-2022, entry version 48.
DE RecName: Full=Aliphatic nitrilase {ECO:0000303|PubMed:26521240};
DE EC=3.5.5.1;
DE AltName: Full=NitSf {ECO:0000303|PubMed:26521240};
GN Name=nit; OrderedLocusNames=SFHH103_06513;
OS Rhizobium fredii (strain HH103) (Sinorhizobium fredii).
OG Plasmid pSfHH103e.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=1117943;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=26521240; DOI=10.1007/s00253-015-7023-1;
RA Vesela A.B., Rucka L., Kaplan O., Pelantova H., Nesvera J., Patek M.,
RA Martinkova L.;
RT "Bringing nitrilase sequences from databases to life: the search for novel
RT substrate specificities with a focus on dinitriles.";
RL Appl. Microbiol. Biotechnol. 100:2193-2202(2016).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HH103; PLASMID=pSfHH103e;
RX PubMed=22374952; DOI=10.1128/jb.06729-11;
RA Weidner S., Becker A., Bonilla I., Jaenicke S., Lloret J., Margaret I.,
RA Puhler A., Ruiz-Sainz J.E., Schneiker-Bekel S., Szczepanowski R.,
RA Vinardell J.M., Zehner S., Gottfert M.;
RT "Genome sequence of the soybean symbiont Sinorhizobium fredii HH103.";
RL J. Bacteriol. 194:1617-1618(2012).
CC -!- FUNCTION: Nitrilase that hydrolyzes preferentially phenylacetonitrile,
CC but not (R,S)-mandelonitrile. Also acts on dinitriles like
CC phenylenediacetonitriles (PDAs) 1,2-PDA, 1,3-PDA, and 1,4-PDA, and
CC cyanophenyl acetonitriles (CPAs) 2-CPA and 4-CPA, but with lower
CC activities. {ECO:0000269|PubMed:26521240}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a nitrile + 2 H2O = a carboxylate + NH4(+);
CC Xref=Rhea:RHEA:21724, ChEBI:CHEBI:15377, ChEBI:CHEBI:18379,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:29067; EC=3.5.5.1;
CC Evidence={ECO:0000269|PubMed:26521240};
CC -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC Nitrilase family. {ECO:0000305}.
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DR EMBL; LN875499; CTQ87323.1; -; Genomic_DNA.
DR EMBL; HE616899; CCF00972.1; -; Genomic_DNA.
DR RefSeq; WP_014332611.1; NC_016815.1.
DR AlphaFoldDB; G9AIU0; -.
DR SMR; G9AIU0; -.
DR KEGG; sfh:SFHH103_06513; -.
DR PATRIC; fig|380.5.peg.6056; -.
DR HOGENOM; CLU_030130_6_1_5; -.
DR OMA; PKGLDFG; -.
DR Proteomes; UP000007735; Plasmid pSfHH103e.
DR GO; GO:0080061; F:indole-3-acetonitrile nitrilase activity; IEA:UniProtKB-EC.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR CDD; cd07564; nitrilases_CHs; 1.
DR Gene3D; 3.60.110.10; -; 1.
DR InterPro; IPR003010; C-N_Hydrolase.
DR InterPro; IPR036526; C-N_Hydrolase_sf.
DR InterPro; IPR000132; Nitrilase/CN_hydratase_CS.
DR InterPro; IPR044149; Nitrilases_CHs.
DR PANTHER; PTHR46044; PTHR46044; 1.
DR Pfam; PF00795; CN_hydrolase; 1.
DR SUPFAM; SSF56317; SSF56317; 1.
DR PROSITE; PS50263; CN_HYDROLASE; 1.
DR PROSITE; PS00921; NITRIL_CHT_2; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Plasmid.
FT CHAIN 1..308
FT /note="Aliphatic nitrilase"
FT /id="PRO_0000451138"
FT DOMAIN 4..270
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 44
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 130
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 164
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
SQ SEQUENCE 308 AA; 33301 MW; 95ABC2D07F475D37 CRC64;
MTKFRAAVVQ AAPVPNDVEA TIEKTINLIR EAAARGANVA VFPEAFIGGY PKGANFNIHI
GARTPEGRQE FADYRAGAIA VPGSETEQLA QAAHEAGLYL TIGVIERDGG TLYCTALYFT
PDGLAGKHRK LMPTGAERLC WGFGDGSTLD TVQTPWGSMG AVICWENYMP LMRTAMYGKG
IALYCAPTAD DRDSWAATMR HIALEGRCFV LSACQYLTRK DFPESMGNRI TDEPDAVLMR
GGAIIVDPLG RVVAGPDYSG ETILTADLDT DDIPRAQFDF DVVGHYARPD VFKLVVDEEP
KSAVVTRA