ID A0A0F4PN81_9GAMM Unreviewed; 553 AA.
AC A0A0F4PN81;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Amidohydrolase {ECO:0000313|EMBL:KJY98480.1};
GN ORFNames=TW72_12130 {ECO:0000313|EMBL:KJY98480.1};
OS Pseudoalteromonas ruthenica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=151081 {ECO:0000313|EMBL:KJY98480.1, ECO:0000313|Proteomes:UP000033664};
RN [1] {ECO:0000313|EMBL:KJY98480.1, ECO:0000313|Proteomes:UP000033664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S3137 {ECO:0000313|EMBL:KJY98480.1,
RC ECO:0000313|Proteomes:UP000033664};
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:KJY98480.1}.
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DR EMBL; JXXZ01000010; KJY98480.1; -; Genomic_DNA.
DR RefSeq; WP_045979622.1; NZ_PNCF01000022.1.
DR AlphaFoldDB; A0A0F4PN81; -.
DR GeneID; 58229239; -.
DR PATRIC; fig|151081.8.peg.2257; -.
DR eggNOG; COG1574; Bacteria.
DR OrthoDB; 9031471at2; -.
DR Proteomes; UP000033664; 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; IMIDAZOLONEPROPIONASE; 1.
DR PANTHER; PTHR22642:SF2; PROTEIN LONG AFTER FAR-RED 3; 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:KJY98480.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033664};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..553
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002474285"
FT DOMAIN 71..547
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 553 AA; 61124 MW; A6E53BAFE5C932AE CRC64;
MMKNKLVALL MMCSVPYTVL AQTTVIHNIK GYTPTQKGEL ETFATLVIKD GRVINRGKAQ
LSKSYPDAKR IDGQGKVLLP GLIDAHGHII GLGQNLMQLD LRGATSVAEV GKRLQAFAAQ
SEQPWIIGRG WNQELWPGKT FASAADLDKF VSDRPVVLSR VDGHAIWVNS KAMELAGLDS
EVTSPAGGEI IRTAQGSPSG VFIDKAEQLI TAHIPKHSEK ALATALDKAG QHLLSLGITS
AHDAGIDFDT WQLYKQRAKD NNLPLRIYAM LGATDDKLET MLKAGKVDDN EDMLAIRSVK
VYADGALGSR GAALLQDYAD RKGHRGLMLE DQQQLEDIFS LCFKHGFSAH THAIGDRANQ
IVLNAYENVF KRTGGILLRN RIEHAQIVDT DDIPRFKALK IIPSMQPVHA TSDMHMAEQR
LSDSQLAGAY AWRTFLEQGS RVAAGSDFPV ELANPFHGLY SAITRQDHQG LPEQGWRPKE
LLTREQALRA FTLDAAYSAF QEFKVGSLEK GKWADFILVD TDIIHAPVQQ VWQTKVLETW
LAGQRRYQRQ PAL
//
