ID Q63N55_BURPS Unreviewed; 632 AA.
AC Q63N55;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=Amidohydrolase 3 domain-containing protein {ECO:0000259|Pfam:PF07969};
GN OrderedLocusNames=BPSS0441 {ECO:0000313|EMBL:CAH37897.1};
OS Burkholderia pseudomallei (strain K96243).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=272560 {ECO:0000313|EMBL:CAH37897.1, ECO:0000313|Proteomes:UP000000605};
RN [1] {ECO:0000313|EMBL:CAH37897.1, ECO:0000313|Proteomes:UP000000605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K96243 {ECO:0000313|EMBL:CAH37897.1,
RC ECO:0000313|Proteomes:UP000000605};
RX PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.M., Atkins T.,
RA Crossman L.C., Pitt T., Churcher C., Mungall K., Bentley S.D., Sebaihia M.,
RA Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A., Brown N.F.,
RA Challis G.L., Cherevach I., Chillingworth T., Cronin A., Crosset B.,
RA Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z., Hauser H.,
RA Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S., Price C.,
RA Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M.,
RA Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., Whitehead S.,
RA Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT pseudomallei.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
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DR EMBL; BX571966; CAH37897.1; -; Genomic_DNA.
DR RefSeq; WP_004529950.1; NZ_CP009537.1.
DR RefSeq; YP_110464.1; NC_006351.1.
DR AlphaFoldDB; Q63N55; -.
DR STRING; 272560.BPSS0441; -.
DR GeneID; 56531109; -.
DR KEGG; bps:BPSS0441; -.
DR PATRIC; fig|272560.51.peg.6582; -.
DR eggNOG; COG1574; Bacteria.
DR Proteomes; UP000000605; Chromosome 2.
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:SF23; AMIDOHYDROLASE YTCJ-RELATED; 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:UP000000605}.
FT DOMAIN 56..540
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 632 AA; 68926 MW; F857CDAFB8296C9E CRC64;
MADTAARPTP DLILHRGRFT TLDRAHPLAS AVAIKDGRFV AVGGDEILAS AGPATRIVDL
QGKGVLPGLI DNHLHIIRGG LNFNMELRWD GVRSLADAMA MLRRQVAVTP APQWVRVVGG
FTEHQFAEKR LPTIDELNAA APDTPVFILH LYDRALLNGA ALRAVGYTKD TPEPPGGQIV
RDAAGNPTGL LLARPNAAIL YATLAKGPKL PFDYQLNSTR HFMRELNRLG VTGAIDAGGG
FQNYPDDYAV IERLAKDGQL TIRLAYNLFT QKPKEEKQDF LNWTASSTYH DGTDYFRHNG
AGEMLVFSAA DFEDFREPRP DLPAQMEGEL EAVVRVLAQN RWPWRLHATY DETIRRALDV
FERVNRDIPL AGLNWFFDHA ETISDESIDR IAALGGGIAV QHRMAYQGEY FVERYGAAAA
EATPPVARML ERGVNVSAGT DATRVASYNP WVSLAWLVTG KTVGGMSLYP RANCIDRETA
LRMWTEHVTW FSNEVGKKGR IQVGQLADLI VPDRDFFACP ESDIADTTSL LTVVGGKVVY
GAGPFADLDE GAPPPAMPDW SPARTFGGYA GWADREGGAP LQQVVRQAAQ SCACANSCGV
HAHRHASAWG SSLPVADLKS FWGALGCSCW AV
//
