ID A0A0I9U6X2_9MYCO Unreviewed; 534 AA.
AC A0A0I9U6X2;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Amidohydrolase {ECO:0000313|EMBL:KLO38016.1};
GN ORFNames=ABH38_05290 {ECO:0000313|EMBL:KLO38016.1};
OS Mycobacterium haemophilum.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=29311 {ECO:0000313|EMBL:KLO38016.1, ECO:0000313|Proteomes:UP000036334};
RN [1] {ECO:0000313|EMBL:KLO38016.1, ECO:0000313|Proteomes:UP000036334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UC1 {ECO:0000313|Proteomes:UP000036334};
RA Greninger A.L., Cunningham G., Miller S.;
RT "Genome sequence of Mycobacterium haemophilum.";
RL Submitted (MAY-2015) 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:KLO38016.1}.
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DR EMBL; LDPR01000003; KLO38016.1; -; Genomic_DNA.
DR RefSeq; WP_047313600.1; NZ_LDPT01000007.1.
DR AlphaFoldDB; A0A0I9U6X2; -.
DR STRING; 1202450.B586_19265; -.
DR PATRIC; fig|29311.18.peg.1815; -.
DR OrthoDB; 3173428at2; -.
DR Proteomes; UP000036334; 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:KLO38016.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000036334}.
FT DOMAIN 51..532
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
FT REGION 161..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 534 AA; 57420 MW; 93D3A236039D3B84 CRC64;
MADADIVITG NVLTVDDVRP TAEALAVADG RIIAVGNRSE IAKFIGTGTV TIDVGAGCVM
PGFVEAHGHP LMEAVALSDR IVDIRPVTMR NADDVVEAVR RETAARGAAG AYLIGWDLLL
QPGLPQPTLS WLDDIAPDGP LVIIHNSGHK AYFNSHAARR AGLNTDTPDP KGAKYGRDGD
GELDGTAEET GAVFPLLGGA IEPSDYPAML RAECARLNRA GLTTCSEMAF DPVFRPLVEQ
LRDELTVRLR SYEISNPQLS TDATPGEGDD MLRQVGIKIW VDGSPWVGNI ALSFPYLDTA
ATRAIGVPAG SCGHANYTRD QLTEIVGAYF PLGWPLACHV HGDAGVDTIL DVYEEALRRH
PRPDHRLRLE HVGAIRPDQL QRAAGLGVTC SMFVDQIHYW GDVIIDGLFG PERGSRWMPA
GSAVATGMRI SLHNDPPVTP EEPLRNISVA ATRVAPSGRV LAPEERLTVD QAIRAQTIDA
AWQLFADDVI GSLEVGKYAD MVVLSADPRT VPPERIADLE VRATFLAGRQ VYPQ
//
