ID E6VIG7_RHOPX Unreviewed; 210 AA.
AC E6VIG7;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=nitrile hydratase {ECO:0000256|ARBA:ARBA00013079};
DE EC=4.2.1.84 {ECO:0000256|ARBA:ARBA00013079};
GN OrderedLocusNames=Rpdx1_2699 {ECO:0000313|EMBL:ADU44285.1};
OS Rhodopseudomonas palustris (strain DX-1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=652103 {ECO:0000313|EMBL:ADU44285.1, ECO:0000313|Proteomes:UP000001402};
RN [1] {ECO:0000313|Proteomes:UP000001402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DX-1 {ECO:0000313|Proteomes:UP000001402};
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Misra M., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Logan B., Oda Y., Harwood C.,
RA Woyke T.;
RT "Complete sequence of Rhodopseudomonas palustris DX-1.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
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}.
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; CP002418; ADU44285.1; -; Genomic_DNA.
DR AlphaFoldDB; E6VIG7; -.
DR STRING; 652103.Rpdx1_2699; -.
DR KEGG; rpx:Rpdx1_2699; -.
DR eggNOG; ENOG502Z7U0; Bacteria.
DR HOGENOM; CLU_092054_0_0_5; -.
DR OrthoDB; 528553at2; -.
DR BioCyc; RPAL652103:RPDX1_RS13270-MONOMER; -.
DR Proteomes; UP000001402; Chromosome.
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, ECO:0000313|EMBL:ADU44285.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR001426-1}.
FT DOMAIN 18..199
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 210 AA; 23332 MW; 3F3B5C8AF0475B27 CRC64;
MSNEHRHHHD HDHSELSETE LRVRALETIL TEKGYVDPAA LDALIETYET KVGPRNGARV
VAKAWSDPAY RQRLLHDATA AIAELGYTGR QGEHIVAVEN TPATHNMVVC TLCSCYPWPV
LGLPPVWYKS APYRSRVVKE PRAVLAEFGV TLPQDITIRV WDSTAEIRYL VIPMRPDGSD
GLSEDRLADL VTRDSMIGTG LARQPSEVAA
//
