ID A0A0Q2LR93_MYCGO Unreviewed; 579 AA.
AC A0A0Q2LR93;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Amidohydrolase {ECO:0000313|EMBL:KQH78210.1};
GN ORFNames=AO501_02270 {ECO:0000313|EMBL:KQH78210.1};
OS Mycobacterium gordonae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1778 {ECO:0000313|EMBL:KQH78210.1, ECO:0000313|Proteomes:UP000051677};
RN [1] {ECO:0000313|EMBL:KQH78210.1, ECO:0000313|Proteomes:UP000051677}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CTRI 14-8773 {ECO:0000313|EMBL:KQH78210.1,
RC ECO:0000313|Proteomes:UP000051677};
RA Ustinova V., Smirnova T., Blagodatskikh K., Varlamov D., Larionova E.,
RA Chernousova L.;
RT "Mycobacterium gordonae draft genome assembly.";
RL Submitted (OCT-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:KQH78210.1}.
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DR EMBL; LKTM01000223; KQH78210.1; -; Genomic_DNA.
DR RefSeq; WP_055578672.1; NZ_LKTM01000223.1.
DR AlphaFoldDB; A0A0Q2LR93; -.
DR STRING; 1778.A9W97_20960; -.
DR OrthoDB; 9766983at2; -.
DR Proteomes; UP000051677; Unassembled WGS sequence.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR CDD; cd01297; D-aminoacylase; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 2.
DR InterPro; IPR013108; Amidohydro_3.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR11647:SF99; D-PHENYLHYDANTOINASE-RELATED; 1.
DR PANTHER; PTHR11647; HYDRANTOINASE/DIHYDROPYRIMIDINASE FAMILY MEMBER; 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:KQH78210.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051677}.
FT DOMAIN 45..554
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
FT REGION 560..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 579 AA; 61766 MW; 790D6837C8545F5F CRC64;
MTYDLLIRNG TIVDGLGGEP YVGDVAVKDG LIAAVGAVNG ASATREIDAS GLLVTPGFVD
LHTHYDGQAI WSDRLTPSSA HGVTTVVMGN CGVGFAPCRQ EDHDVLVDVM AGVEDIPGVV
MTDGLPWTWE TFPEYLDALE SGRRDIDVAA YLPHSPLRVY VMGQRGADRE PATAEDLAKM
RALATEAIEV GALGFASSRL TIHKTESGAP IPSYDAAREE IEEIARGVVD GGGGLLQFVP
DIPAGGYQPV LQTVFDVAED VGLPVTFTLV VGNAGDPTWP DAITMVEKAN ARAGAGDPQV
TAQLLPRPIG LIIGLQLTAN PFVLYPSYRE IAHLPLAERV AEMRKPEVRA RILADKPGQG
HPILYVAQMW DWIFPLDDNP NYEPNPADSI GARARARGVD PMEEAYDRLL DDDGRAMLLV
ATSNLERNSL DTVGKLLHRD DVVLGLGDGG AHYGMICDAS YSTYFLTHWA RDRKSGRFSV
AEAVRELTSV PARIAGLADR GRIAAGFKAD LNVIDHAALR LHKPVIAHDL PAGGRRLDQT
AQGYVATVVS GEVIAENGVP TSARPGKLVR GRQSAPAPA
//
