ID A0A0F6A6Q7_9GAMM Unreviewed; 579 AA.
AC A0A0F6A6Q7;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Amidohydrolase 3 domain-containing protein {ECO:0000259|Pfam:PF07969};
GN ORFNames=N479_20855 {ECO:0000313|EMBL:KKE81887.1};
OS Pseudoalteromonas luteoviolacea S4054.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=1129367 {ECO:0000313|EMBL:KKE81887.1, ECO:0000313|Proteomes:UP000033434};
RN [1] {ECO:0000313|EMBL:KKE81887.1, ECO:0000313|Proteomes:UP000033434}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S4054 {ECO:0000313|EMBL:KKE81887.1,
RC ECO:0000313|Proteomes:UP000033434};
RX PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT bacteria.";
RL BMC Genomics 16:158-158(2015).
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:KKE81887.1}.
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DR EMBL; AUXW01000175; KKE81887.1; -; Genomic_DNA.
DR RefSeq; WP_046357646.1; NZ_AUXW01000175.1.
DR AlphaFoldDB; A0A0F6A6Q7; -.
DR PATRIC; fig|1129367.4.peg.4245; -.
DR Proteomes; UP000033434; 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:SF23; AMIDOHYDROLASE YTCJ-RELATED; 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;
FT DOMAIN 97..577
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 579 AA; 63734 MW; 9B32B60B939F063C CRC64;
MRVTNMSLLP IIVAGLCISG CNSDSSSTAN NSVNSNTPTT TPNQTAQVQS TMVFVNGDIY
TVNEAKPWAQ AIAIKDNKII FVGSTEQAQQ HIGENTQVID LKGKMMMPGF HDVHMHPLES
GSDATQFTIP EEESTETYID LIADAAFQNP DAEWLIGYGH SIGTLLEMQD SPIEVLDEAV
PNRPVIIMEQ TSHSMWVNSK ALELARINAN SLDPIGGVIG RDEQGNVDGI LYDNAGNQVM
ELAMRSLTNT QQNDYLGLID YTMPALNKAG ITSISDARTY WQRGHLDTWL KIAKEDKLTL
RAHLGLWAYP QMNDATQLSK LKSLYQADPN SLLKVNQVKF YVDGILVNTT AAMHEPYHQN
WLELDGNNGL NYFTQARLEK YIKALEPTGF DFNIHAIGDR GIHEALNAIE NASSGKARHR
LTHLEVVDPA DYGRFAKLGV IADAQVAGDF TDPNHWPENI PLLGAERSQD LVPIKNLVDS
NATLTLSSDW NVSPFNPFIG ISNAISRAPQ AITLAQALEA YTLNSAYAMR QDHLVGSIEV
GKLADLVVLD KNLFESTVKE IANTQVTMTL LDGEIVYQR
//
