ID A0A2P8FHJ3_9RHOB Unreviewed; 571 AA.
AC A0A2P8FHJ3;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Amidohydrolase 3 domain-containing protein {ECO:0000259|Pfam:PF07969};
GN ORFNames=CLV88_102285 {ECO:0000313|EMBL:PSL21165.1};
OS Shimia abyssi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae.
OX NCBI_TaxID=1662395 {ECO:0000313|EMBL:PSL21165.1, ECO:0000313|Proteomes:UP000240418};
RN [1] {ECO:0000313|EMBL:PSL21165.1, ECO:0000313|Proteomes:UP000240418}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100673 {ECO:0000313|EMBL:PSL21165.1,
RC ECO:0000313|Proteomes:UP000240418};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-2018) 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:PSL21165.1}.
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DR EMBL; PYGJ01000002; PSL21165.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P8FHJ3; -.
DR OrthoDB; 9811399at2; -.
DR Proteomes; UP000240418; 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 Reference proteome {ECO:0000313|Proteomes:UP000240418};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..571
FT /note="Amidohydrolase 3 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015184969"
FT DOMAIN 74..564
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 571 AA; 61364 MW; 57B99395C87AAE96 CRC64;
MTHFSRLISA LIGAAVLATP VLAQDIADRI YTGGPILTMS DHAPRAQAVA VKNGHILAVG
SLSDVRPHWG DSTQTYDLAG RTLLPGFVDS HGHAVMGGLQ ALSANLLAAP DGNVSDIASL
LDTLRGWTAD HQATVDATNL IVGFGYDQSQ LAELRHPTRA DLDQVSADIP IIIVHQSGHF
GAANSAALAL AGITADSENP PGGIIRFDDT GLPNGVLEEN AFFIVLGALL DGLGEEGFKS
FARAGVDLWA SFGYTTAQEG RATPQVAAIV DMVAAETPLP IDVVVYADVL VDREFVAQNH
GHEYQNRVRI GGAKLTIDGS PQGFTALRDR PYYDPVGDYA AGYRGYASAT MQQVTDAIDW
AFANNVQILT HANGEGASDM LIAAVDAATL SHGVADRRPV LIHGQFLRPD QVDSYKRLGV
FPSLFPMHTF YWGDWHRDHT VGPENADNIS PTGWLRQRDM IFGTHHDAPV AFPDSMRVLS
ATVTRRTRSG DILGPHQRVD AMTALKAMTI WPAWQHFEEG SKGSLEPGKL ADFVILSDDP
TAVDPEILAN LKVLATIKED KVVFDALKRD E
//