ID   A0A1H9QJY0_9SPHN        Unreviewed;       566 AA.
AC   A0A1H9QJY0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Amidohydrolase 3 domain-containing protein {ECO:0000259|Pfam:PF07969};
GN   ORFNames=SAMN05518866_114115 {ECO:0000313|EMBL:SER60891.1};
OS   Sphingobium sp. YR768.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=1884365 {ECO:0000313|EMBL:SER60891.1, ECO:0000313|Proteomes:UP000199142};
RN   [1] {ECO:0000313|Proteomes:UP000199142}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YR768 {ECO:0000313|Proteomes:UP000199142};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FOGE01000014; SER60891.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9QJY0; -.
DR   STRING; 1884365.SAMN05518866_114115; -.
DR   OrthoDB; 9811399at2; -.
DR   Proteomes; UP000199142; 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   Reference proteome {ECO:0000313|Proteomes:UP000199142};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..566
FT                   /note="Amidohydrolase 3 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011726664"
FT   DOMAIN          87..562
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
FT   REGION          60..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..76
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   566 AA;  61488 MW;  70DF128A81EA512E CRC64;
     MRAAALAAIA ALALPLPAHA SGVIDNVNGI AIDANGKLVH FDALMVDDDG KVEKLIQGRY
     QEPEYKPKKP KKGQPWPERP KPLSFRMDAG GKTLIPGLID GHGHVMGYGM ALITLDLSDT
     KSLAEAQAKI RAYVEANPGR KWIIGTGWNQ EQWGLGRFPT AAELDAAESE TPVWLERVDG
     HAGWANSAAI RAAGITATTK APMGGRIEMA AGKPAGVFVD KAMSLIQKFV PPPAPKDRDN
     ALEKAQRALL SMGITGIADM GTSIEDWQAF RRSADRGALR VRIMSYAYGI DNMVLIAGSE
     PTPWLYDDRL RMGGIKLLLD GALGSRGAWL RADYADAPGQ RGLPMIPDTQ LRNFMSRAAM
     DNFQVAVHAI GDAANHEVLN AIEELNDTYK GDRRWRIEHA QIIDPADLPR FKPLGVVASM
     QPVHEASDWR MATARMGEAR LKGAYAWKTM LDNGVPLAFG SDVPVESPNP FPGIAVAMTR
     EDAKGEPAGG WMPEQRIGFE AALDGFTRQA AYAGFAEKRF GNLAVGQRAD FLLIDRDIST
     TRPADIRQTQ VLETWIGGKR VYVKGQ
//