ID D4XCZ2_9BURK Unreviewed; 629 AA.
AC D4XCZ2;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Amidohydrolase family protein {ECO:0000313|EMBL:EFF75208.1};
GN ORFNames=HMPREF0004_3339 {ECO:0000313|EMBL:EFF75208.1};
OS Achromobacter piechaudii ATCC 43553.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=742159 {ECO:0000313|EMBL:EFF75208.1, ECO:0000313|Proteomes:UP000004510};
RN [1] {ECO:0000313|Proteomes:UP000004510}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43553 {ECO:0000313|Proteomes:UP000004510};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R., Gibbs R.;
RT "Complete sequence of Mobiluncus curtisii ATCC 43063.";
RL Submitted (MAR-2010) 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:EFF75208.1}.
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DR EMBL; ADMS01000077; EFF75208.1; -; Genomic_DNA.
DR RefSeq; WP_006219416.1; NZ_GG770409.1.
DR AlphaFoldDB; D4XCZ2; -.
DR PATRIC; fig|742159.3.peg.4329; -.
DR eggNOG; COG1574; Bacteria.
DR HOGENOM; CLU_009942_4_3_4; -.
DR OrthoDB; 9031471at2; -.
DR Proteomes; UP000004510; 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: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 Hydrolase {ECO:0000313|EMBL:EFF75208.1}.
FT DOMAIN 54..537
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 629 AA; 68638 MW; B9276A46B3CAC71E CRC64;
MADTQAPDLI LHQGRFTTLD PANPVADAVA IHDGRFTRVG AAADILPLAG PATKVIALNG
RGVLPGLIDN HLHIIRGGLN YNMELRWDGV RSLADAMAML RRQVAITPAP QWVRVVGGFT
EHQFAEKRLP TIEELNAVAP DTPVFILHLY DRALLNAAAL RAVGYDKSTP APPGGEIVRD
SAGNPTGLLL AKPNASILYA TLAKGPKLPM EYQVNSTRHF MRELNRLGVT GAIDAGGGFQ
NYPEDYQVIQ QLADAGQLTI RLAYNLFTQK PKQEKEDFLN WAATSQYKQG TDYFRHNGAG
EMLVFSAADF EDFRQPRPEM APEMEGELEE VVRILAQNRW PWRMHATYDE TISRALDVFE
RVNRDVPLAG LNWFFDHAET ISEKSIDRIA ALGGGVAVQH RMAYQGEYFV ERYGAGAAEA
TPPVKRMLEK GVNVSAGTDA TRVASYNPWV SLSWLITGKT VGGLRLTPQR NCLDRDAALR
MWTENVTWFS NEQGKKGRIA VGQLADLVVP DRDFFACPES DIADTSSLLT VVGGKVVWGA
GEFSGHDEAA PPPAMPDWSP TRLFGGYGAW GDSEGKPLQT SLRDAAAACA CLNDCNVHGH
QHAGAWASKL PVSDLKGFWG ALGCACWAV
//
