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Database: UniProt
Entry: H1B6T5_9FIRM
LinkDB: H1B6T5_9FIRM
Original site: H1B6T5_9FIRM 
ID   H1B6T5_9FIRM            Unreviewed;       531 AA.
AC   H1B6T5;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Amidohydrolase 3 domain-containing protein {ECO:0000259|Pfam:PF07969};
GN   ORFNames=HMPREF0981_00918 {ECO:0000313|EMBL:EHO31306.1};
OS   Erysipelotrichaceae bacterium 6_1_45.
OC   Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC   Erysipelotrichaceae.
OX   NCBI_TaxID=469614 {ECO:0000313|EMBL:EHO31306.1, ECO:0000313|Proteomes:UP000003818};
RN   [1] {ECO:0000313|EMBL:EHO31306.1, ECO:0000313|Proteomes:UP000003818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=6_1_45 {ECO:0000313|EMBL:EHO31306.1,
RC   ECO:0000313|Proteomes:UP000003818};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA   Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA   Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Goldberg J.,
RA   Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA   MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Erysipelotrichaceae bacterium 6_1_45.";
RL   Submitted (OCT-2011) 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:EHO31306.1}.
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DR   EMBL; ACTK01000017; EHO31306.1; -; Genomic_DNA.
DR   AlphaFoldDB; H1B6T5; -.
DR   PATRIC; fig|469614.3.peg.923; -.
DR   HOGENOM; CLU_009942_2_1_9; -.
DR   BioCyc; EBAC469614-HMP:GMFG-918-MONOMER; -.
DR   Proteomes; UP000003818; 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;
FT   DOMAIN          45..521
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   531 AA;  59911 MW;  256031A5B8B96357 CRC64;
     MIQILNARIL TMKDRQTASC MCIEHGSIVY IGDHIPEEYK AADCVDMGGR VIIPGIIDAH
     SHLVSCANTF RQADLSNARS FADIQHILTD FIQQHHLKEQ DWVSGVGYDH TLLKERRHPD
     ADVLKAVGRR PIVITHASSH MGVASYTAMQ LANIPPDAPN PVGGRYGRNT DGMLNGYMEE
     NAFTSFLHHV PMPSIEEMMR LLEDALQLYA SYGITTIQDG MMNAAVYAIL KEAAARNILK
     QDVVGYVGIR DSEALRKESK PKGVQYHKHF RIGGYKMFLD GSPQGRTAWM QTPYQGDANY
     YGYGTMSDEE VAACIRKSLL EHQQLLAHCN GDAAAEQYLT QFEKIVRELD AKDTLRPVMI
     HAQLVQKEQL ERMKPLQMIP SFFAAHVWHW GDVHIENFGV QRASLISPLR DALQLGLVFT
     LHTDTPVIAP NLMESVWCAA VRRTKNGVLL GEKERIDVYE ALRAITQYAA WQYHEEDQKG
     TLEAGKLADF AVLDQNPLEI PVEEIRNIQV LETWKEGTCM YKRQVQESQN I
//
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