ID K0IAH1_9BURK Unreviewed; 271 AA.
AC K0IAH1;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE SubName: Full=Nitrilase/cyanide hydratase and apolipoprotein n-acyltransferase {ECO:0000313|EMBL:AFU48309.1};
GN ORFNames=C380_23085 {ECO:0000313|EMBL:AFU48309.1};
OS Acidovorax sp. KKS102.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=358220 {ECO:0000313|EMBL:AFU48309.1, ECO:0000313|Proteomes:UP000006306};
RN [1] {ECO:0000313|EMBL:AFU48309.1, ECO:0000313|Proteomes:UP000006306}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KKS102 {ECO:0000313|EMBL:AFU48309.1,
RC ECO:0000313|Proteomes:UP000006306};
RX PubMed=23209225; DOI=10.1128/JB.01848-12;
RA Ohtsubo Y., Maruyama F., Mitsui H., Nagata Y., Tsuda M.;
RT "Complete Genome Sequence of Acidovorax sp. Strain KKS102, a
RT Polychlorinated-Biphenyl Degrader.";
RL J. Bacteriol. 194:6970-6971(2012).
CC -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC NIT1/NIT2 family. {ECO:0000256|ARBA:ARBA00010613}.
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; CP003872; AFU48309.1; -; Genomic_DNA.
DR RefSeq; WP_015016251.1; NC_018708.1.
DR AlphaFoldDB; K0IAH1; -.
DR STRING; 358220.C380_23085; -.
DR KEGG; ack:C380_23085; -.
DR PATRIC; fig|358220.3.peg.4713; -.
DR eggNOG; COG0388; Bacteria.
DR HOGENOM; CLU_030130_1_2_4; -.
DR OrthoDB; 9811121at2; -.
DR Proteomes; UP000006306; Chromosome.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR CDD; cd07572; nit; 1.
DR Gene3D; 3.60.110.10; Carbon-nitrogen hydrolase; 1.
DR InterPro; IPR003010; C-N_Hydrolase.
DR InterPro; IPR036526; C-N_Hydrolase_sf.
DR InterPro; IPR045254; Nit1/2_C-N_Hydrolase.
DR InterPro; IPR001110; UPF0012_CS.
DR PANTHER; PTHR23088:SF27; DEAMINATED GLUTATHIONE AMIDASE; 1.
DR PANTHER; PTHR23088; NITRILASE-RELATED; 1.
DR Pfam; PF00795; CN_hydrolase; 1.
DR SUPFAM; SSF56317; Carbon-nitrogen hydrolase; 1.
DR PROSITE; PS50263; CN_HYDROLASE; 1.
DR PROSITE; PS01227; UPF0012; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000313|EMBL:AFU48309.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipoprotein {ECO:0000313|EMBL:AFU48309.1};
KW Transferase {ECO:0000313|EMBL:AFU48309.1}.
FT DOMAIN 1..253
FT /note="CN hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS50263"
SQ SEQUENCE 271 AA; 29556 MW; FDCA080DD6450388 CRC64;
MKVAAIQMVS STALDDNLRV ARELLEQAVL GGAELAVLPE YFCLMGYKDT DKLALRETAG
SGVIQQFLAD TARALQIWIV GGTLPMATDA PDRVRNTTLV FDPTGACVAR YDKIHLFRFS
NGAEQYDEGR VIDAGDTPVQ FDLQARSGQR WRVGLSVCYD LRFPELYRAH ARAGADLLLV
PSAFTHTTGQ AHWDVLLRAR AVENLAYVLA PAQGGVHANG RHTWGHSMLV DPWGSILAQR
DQGAGVVAGE LDVQRLSAVR AQLPALTHRV L
//