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Database: UniProt
Entry: A0A1I6HD63_9FLAO
LinkDB: A0A1I6HD63_9FLAO
Original site: A0A1I6HD63_9FLAO 
ID   A0A1I6HD63_9FLAO        Unreviewed;       571 AA.
AC   A0A1I6HD63;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=Amidohydrolase 3 domain-containing protein {ECO:0000259|Pfam:PF07969};
GN   ORFNames=SAMN04490243_2586 {ECO:0000313|EMBL:SFR52389.1};
OS   Robiginitalea myxolifaciens.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Robiginitalea.
OX   NCBI_TaxID=400055 {ECO:0000313|EMBL:SFR52389.1, ECO:0000313|Proteomes:UP000199534};
RN   [1] {ECO:0000313|EMBL:SFR52389.1, ECO:0000313|Proteomes:UP000199534}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21019 {ECO:0000313|EMBL:SFR52389.1,
RC   ECO:0000313|Proteomes:UP000199534};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FOYQ01000002; SFR52389.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6HD63; -.
DR   STRING; 400055.SAMN04490243_2586; -.
DR   OrthoDB; 9767366at2; -.
DR   Proteomes; UP000199534; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000199534};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..571
FT                   /note="Amidohydrolase 3 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011613341"
FT   DOMAIN          78..564
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   571 AA;  63271 MW;  3CE30834D260AFA1 CRC64;
     MRLFRLTLLV ASAVFLACQG EQETESPATM YFNGDILTMV GATPEYVEAL VERDGKILFV
     GDTNKAMQIA GKGHIMKNLQ GATMLPGLID GHAHFANFGL QAVGAQLLAP PDADVANIPK
     LIEVLKAWNT PENRSLTGWI FGTGFDDSVL EEKRFPTRHD LDQVTEEFPI MIMHISGHFA
     VVNSKGLEVL GITAETPDPE GGIIRREANS REPNGVLEEL AAIPNMIAAM MPKTPEANQM
     FFDAGQEMAL SYGYTTAQEG RAMQNHELLT AMASQNKLKI DVVSYIDYMF TDQYMGAEWN
     SKAYTNHYRI GGMKITLDGS PQGRTAWRTK PYLIPPDGMG SEYSGYPAIP DDSTVRSILE
     RGFQNDWQIL AHANGDAAID QLLSTMESLH QQYKPSGRRD VIIHGQYIRE DQLNKAVSLN
     LIGSLFPMHT FYWGDWHKQL IGDSLGNKIS PVRSALDKGL KITLHTDAPV ALPNLMRVVW
     TAVARTSRSG ETIGAEERIT PYEALQSITS WSAFQHFEED QKGTLEPGKL ADLVILDNNP
     LKVPAAEIKN IQVMETIKEG ETVYQRSTEQ Q
//
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