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Database: UniProt
Entry: V7J6V1_MYCAV
LinkDB: V7J6V1_MYCAV
Original site: V7J6V1_MYCAV 
ID   V7J6V1_MYCAV            Unreviewed;       583 AA.
AC   V7J6V1;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Amidohydrolase {ECO:0000313|EMBL:ETA93321.1};
GN   ORFNames=O982_22225 {ECO:0000313|EMBL:ETA93321.1};
OS   Mycobacterium avium 10-5581.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=1392000 {ECO:0000313|EMBL:ETA93321.1, ECO:0000313|Proteomes:UP000018557};
RN   [1] {ECO:0000313|EMBL:ETA93321.1, ECO:0000313|Proteomes:UP000018557}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=10-5581 {ECO:0000313|EMBL:ETA93321.1,
RC   ECO:0000313|Proteomes:UP000018557};
RA   Bannantine J.P., Robbe-Austerman S., O'Connell C.;
RT   "Genome sequence of MAC strains.";
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ETA93321.1}.
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DR   EMBL; AYNT01000230; ETA93321.1; -; Genomic_DNA.
DR   AlphaFoldDB; V7J6V1; -.
DR   PATRIC; fig|1392000.4.peg.4729; -.
DR   Proteomes; UP000018557; Unassembled WGS sequence.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   CDD; cd01300; YtcJ_like; 1.
DR   Gene3D; 3.10.310.70; -; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR   InterPro; IPR013108; Amidohydro_3.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR033932; YtcJ-like.
DR   PANTHER; PTHR22642:SF25; EXOENZYMES REGULATORY PROTEIN; 1.
DR   PANTHER; PTHR22642; IMIDAZOLONEPROPIONASE; 1.
DR   Pfam; PF07969; Amidohydro_3; 1.
DR   SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:ETA93321.1}.
FT   DOMAIN          99..581
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   583 AA;  62952 MW;  D42DCC865F3D7B68 CRC64;
     MGWRSSSSPM AWLLLIAWLC IVAGATHGAR LERVAIPVSR TLGPIASVHM GQADLVLTGT
     VLTVDEARPT AEALAVADGR IVAVGTRAEI AAHVGPHTQT VDIGDGCVMP GFVEAHGHPL
     MEAVALSDRI VDIRPVTLAN ADDVVAAVKS EVGKRGEAGA YLNGWDPLLQ QGLPQPTLAW
     LDDIAPDGPL VIIHNSGHKA FFNSRAAQRH GLNRDIPDPK GARYGRDADG ELDGTAEETG
     AVFPLLDGAI DTAGYPRMLH AECARLNRAG LTTCSEMAFD PRFRPLVEQL RGQLTVRLRS
     YEISNPQLRT DATPGEGDDM LRQVGIKIWV DGSPWIGNIA LSFPYLDTEA TRTIGVTPGS
     CGCANYTKEQ LHEIVSAYFP LGWQLACHVQ GDAGVGTILD VYEEALKRHP RDDHRLRLEH
     VGAIRPDQLQ RAADLGVTCS IFVDQIHYWG DVLVDGLFGE ERGSRWMPAG SAVATGMRIS
     LHNDPPVTPE EPLRNISVAA TRKAPSGRVL APEERLTVEQ AIRAQTLDAA WQLFADDVIG
     SLELGKYADL VVLSADPRAV PPERIADLQV RATYLAGRRV YPQ
//
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