ID Q6XMS0_RHOER Unreviewed; 207 AA.
AC Q6XMS0;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 13-SEP-2023, entry version 50.
DE RecName: Full=nitrile hydratase {ECO:0000256|ARBA:ARBA00013079};
DE EC=4.2.1.84 {ECO:0000256|ARBA:ARBA00013079};
OS Rhodococcus erythropolis (Arthrobacter picolinophilus).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus; Rhodococcus erythropolis group.
OX NCBI_TaxID=1833 {ECO:0000313|EMBL:AAP57646.1};
RN [1] {ECO:0000313|EMBL:AAP57646.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=870-AN019 {ECO:0000313|EMBL:AAP57646.1};
RX PubMed=14532022; DOI=10.1128/AEM.69.10.5754-5766.2003;
RA Brandao P.F., Clapp J.P., Bull A.T.;
RT "Diversity of nitrile hydratase and amidase enzyme genes in Rhodococcus
RT erythropolis recovered from geographically distinct habitats.";
RL Appl. Environ. Microbiol. 69:5754-5766(2003).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aliphatic amide = a nitrile + H2O; Xref=Rhea:RHEA:12673,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:18379, ChEBI:CHEBI:65285; EC=4.2.1.84;
CC Evidence={ECO:0000256|ARBA:ARBA00001410};
CC -!- SIMILARITY: Belongs to the nitrile hydratase subunit alpha family.
CC {ECO:0000256|ARBA:ARBA00009363}.
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DR EMBL; AY223829; AAP57646.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6XMS0; -.
DR GO; GO:0080109; F:indole-3-acetonitrile nitrile hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR Gene3D; 3.90.330.10; Nitrile hydratase alpha /Thiocyanate hydrolase gamma; 1.
DR InterPro; IPR036648; CN_Hdrase_a/SCN_Hdrase_g_sf.
DR InterPro; IPR004232; CN_Hdrtase_a/SCN_Hdrlase_g.
DR InterPro; IPR023900; CN_Hdrtase_asu/SCN_Hdrlase_gsu.
DR InterPro; IPR018141; Nitrile_hydratase_asu.
DR NCBIfam; TIGR01323; nitrile_alph; 1.
DR Pfam; PF02979; NHase_alpha; 1.
DR PIRSF; PIRSF001426; NHase_alpha; 1.
DR SUPFAM; SSF56209; Nitrile hydratase alpha chain; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|PIRSR:PIRSR001426-1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR001426-1}.
FT DOMAIN 21..200
FT /note="Nitrile hydratase alpha /Thiocyanate hydrolase
FT gamma"
FT /evidence="ECO:0000259|Pfam:PF02979"
FT BINDING 110
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000256|PIRSR:PIRSR001426-1"
FT BINDING 113
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000256|PIRSR:PIRSR001426-1"
FT BINDING 114
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000256|PIRSR:PIRSR001426-1"
FT BINDING 115
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000256|PIRSR:PIRSR001426-1"
SQ SEQUENCE 207 AA; 23014 MW; 3F6A21AF7010D6A5 CRC64;
MSVTIDHTTE NAAPAQAPVS DRAWALFRAL DGKGLVPDGY VEGWKKTFEE DFSPRRGAEL
VARAWTDPDF RQLLLTDGTA AVAQYGYLGP QGEYIVAVED TPTLKNVIVC SLCSCTAWPI
LGLPPTWYKS FEYRARVVRE PRKVLFEMGT EIASDVEIRV YDTTAETRYM VLPQRPAGTE
GWSQEQLQEI VTKDCLIGVA VPQVPTV
//