ID   A4J4S3_DESRM            Unreviewed;       273 AA.
AC   A4J4S3;
DT   01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   SubName: Full=Nitrilase/cyanide hydratase and apolipoprotein N-acyltransferase {ECO:0000313|EMBL:ABO50076.1};
GN   OrderedLocusNames=Dred_1548 {ECO:0000313|EMBL:ABO50076.1};
OS   Desulforamulus reducens (strain ATCC BAA-1160 / DSM 100696 / MI-1)
OS   (Desulfotomaculum reducens).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC   Desulforamulus.
OX   NCBI_TaxID=349161 {ECO:0000313|EMBL:ABO50076.1, ECO:0000313|Proteomes:UP000001556};
RN   [1] {ECO:0000313|EMBL:ABO50076.1, ECO:0000313|Proteomes:UP000001556}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MI-1 {ECO:0000313|EMBL:ABO50076.1,
RC   ECO:0000313|Proteomes:UP000001556};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.;
RT   "Complete sequence of Desulfotomaculum reducens MI-1.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC       NIT1/NIT2 family. {ECO:0000256|ARBA:ARBA00010613}.
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DR   EMBL; CP000612; ABO50076.1; -; Genomic_DNA.
DR   RefSeq; WP_011877892.1; NC_009253.1.
DR   AlphaFoldDB; A4J4S3; -.
DR   STRING; 349161.Dred_1548; -.
DR   KEGG; drm:Dred_1548; -.
DR   eggNOG; COG0388; Bacteria.
DR   HOGENOM; CLU_030130_3_8_9; -.
DR   OrthoDB; 9811121at2; -.
DR   Proteomes; UP000001556; Chromosome.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR   CDD; cd07584; nitrilase_6; 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; IPR001110; UPF0012_CS.
DR   PANTHER; PTHR43674:SF2; BETA-UREIDOPROPIONASE; 1.
DR   PANTHER; PTHR43674; NITRILASE C965.09-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:ABO50076.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Lipoprotein {ECO:0000313|EMBL:ABO50076.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001556};
KW   Transferase {ECO:0000313|EMBL:ABO50076.1}.
FT   DOMAIN          5..245
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS50263"
SQ   SEQUENCE   273 AA;  30325 MW;  A5D0CCE6F0FCBAE6 CRC64;
     MKRPLTIGLI QMDCVLGDVA ANVAKAIERI RQAAAMGAQI ICLPELCTTG YRPDLLEDKL
     WELTEPVPGP TTDVFSQLAK ELGIYIILPM NEKGAVPGMI HNSAVFIDKD GEVQGVFRKA
     HAYATERYYF TDGNHYPVFQ TEFGKVGVMI CYDMGFPEVA RILTLKGAEV IFAPSAWRQE
     DEDIWDINIA ARALENRLFV AAVNRVGREG DVVMHGKSKI ANTRGKTLAE AARFEEDILV
     ATVDLHELIA GRRETPYLKD RKPASYGLIT QIN
//