ID A0A1H9VG24_9BACI Unreviewed; 513 AA.
AC A0A1H9VG24;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Predicted amidohydrolase {ECO:0000313|EMBL:SES20187.1};
GN ORFNames=SAMN05518872_105307 {ECO:0000313|EMBL:SES20187.1};
OS Psychrobacillus sp. OK032.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Psychrobacillus.
OX NCBI_TaxID=1884358 {ECO:0000313|EMBL:SES20187.1, ECO:0000313|Proteomes:UP000199084};
RN [1] {ECO:0000313|EMBL:SES20187.1, ECO:0000313|Proteomes:UP000199084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK032 {ECO:0000313|EMBL:SES20187.1,
RC ECO:0000313|Proteomes:UP000199084};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOGY01000005; SES20187.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9VG24; -.
DR STRING; 1884358.SAMN05518872_105307; -.
DR OrthoDB; 9811121at2; -.
DR Proteomes; UP000199084; Unassembled WGS sequence.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR CDD; cd04301; NAT_SF; 1.
DR CDD; cd07574; nitrilase_Rim1_like; 1.
DR Gene3D; 3.40.630.30; -; 1.
DR Gene3D; 3.60.110.10; Carbon-nitrogen hydrolase; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR003010; C-N_Hydrolase.
DR InterPro; IPR036526; C-N_Hydrolase_sf.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR001110; UPF0012_CS.
DR PANTHER; PTHR23088:SF50; HYDROLASE YHCX; 1.
DR PANTHER; PTHR23088; NITRILASE-RELATED; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR Pfam; PF00795; CN_hydrolase; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF56317; Carbon-nitrogen hydrolase; 1.
DR PROSITE; PS50263; CN_HYDROLASE; 1.
DR PROSITE; PS51186; GNAT; 1.
DR PROSITE; PS01227; UPF0012; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:SES20187.1}.
FT DOMAIN 14..212
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT DOMAIN 228..484
FT /note="CN hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS50263"
SQ SEQUENCE 513 AA; 59368 MW; 2C10AA593FCC7FD7 CRC64;
MSEEFDLSQF EKSMVIRQTT FSDIESILEI QRICFPGMDP WEVAHLRSHL TIFPEGQLVA
ELDGKVIGSC SSLIINFDEY DDRHSWSDVT DAGYITNHNP DGYNLYGIEV MVHPEYRRMK
VGQRLYEGRK DIARQFNLKS IIIGGRIPNY HKHANEMSPR EYVTAVSRHK IYDPVLTFQL
MNGFTLMRIN PNYLPDDKAS AKYATLMEWN NVDYIPLSKR HFKTSYPVRI CAVQYMMRKI
SSFEEFAHQC EYFVDVASDA QSDFVVFPEI FTTQLMSFLD ESSPSQAVRK LTQYTPQYME
LFADLSVRYN INIIAGSHFV EEENEEIYNI AYLFHRDGAI DKQYKIHITP NERKWWGISA
GDSVQVFDTD CGKIAIQICY DIEFPELARI ATDMGANIIF TPFCTEDRQG YLRVRYCAQA
RAVENQIYTV VSGTVGNLPQ TENMDIQYAQ SAIFAPSDFE FARDGIVGET EPNVEMVLIG
DVDLEILRRQ RQDGTVKHLK DRRHDVYGID YKK
//