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Database: UniProt
Entry: A0A1A6C6N5_9GAMM
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Original site: A0A1A6C6N5_9GAMM 
ID   A0A1A6C6N5_9GAMM        Unreviewed;       422 AA.
AC   A0A1A6C6N5;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Dihydroorotase {ECO:0000313|EMBL:OBS10222.1};
GN   ORFNames=Thpro_021272 {ECO:0000313|EMBL:OBS10222.1};
OS   Acidihalobacter prosperus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Acidihalobacter.
OX   NCBI_TaxID=160660 {ECO:0000313|EMBL:OBS10222.1, ECO:0000313|Proteomes:UP000029273};
RN   [1] {ECO:0000313|EMBL:OBS10222.1, ECO:0000313|Proteomes:UP000029273}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5130 {ECO:0000313|EMBL:OBS10222.1,
RC   ECO:0000313|Proteomes:UP000029273};
RX   PubMed=25342676;
RA   Ossandon F.J., Cardenas J.P., Corbett M., Quatrini R., Holmes D.S.,
RA   Watkin E.;
RT   "Draft Genome Sequence of the Iron-Oxidizing, Acidophilic, and Halotolerant
RT   'Thiobacillus prosperus' Type Strain DSM 5130.";
RL   Genome Announc. 2:0-0(2014).
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:OBS10222.1}.
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DR   EMBL; JQSG02000002; OBS10222.1; -; Genomic_DNA.
DR   RefSeq; WP_038088519.1; NZ_JQSG02000002.1.
DR   AlphaFoldDB; A0A1A6C6N5; -.
DR   STRING; 160660.BJI67_03875; -.
DR   OrthoDB; 9807210at2; -.
DR   Proteomes; UP000029273; Unassembled WGS sequence.
DR   GO; GO:0019213; F:deacetylase activity; IEA:InterPro.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR020043; Deacetylase_Atu3266-like.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   PANTHER; PTHR42717; DIHYDROOROTASE-RELATED; 1.
DR   PANTHER; PTHR42717:SF1; DIHYDROOROTASE-RELATED; 1.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   PIRSF; PIRSF039004; ADE_EF_0837; 1.
DR   SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR039004-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029273};
KW   Zinc {ECO:0000256|PIRSR:PIRSR039004-1}.
FT   DOMAIN          60..379
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
FT   BINDING         69
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT   BINDING         71
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT   BINDING         168
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT   BINDING         168
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT   BINDING         201
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT   BINDING         235
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT   BINDING         295
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT   MOD_RES         168
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039004-2"
SQ   SEQUENCE   422 AA;  45119 MW;  9F982DBB97BFC48A CRC64;
     MNQTSTDDYD LILRGGRVID TASGFDAVAD LAIRDGRIAA LAPHLEATPG ARVIDVGGKL
     VTAGLIDTHA HVFQHVTGRF GLNPDLCGVR SGVTTLVDQG GPSLMTLPAF RHYVSEPADS
     SVLCFLSAYL VGGLEGHHYA QLYGPEMVDV KRTIKIGREN RDLVKGIKAH AEIGGKSRWG
     MDVIKQAAEI AVGIDVPLYI HLGQLWPERE KGVVDPDSVI EELVPIMRPG DVLAHPFTRH
     PGGFISTRTG EVHPIVEAAL AQGIRVDVGH GSHFSFEMAE KVLAHGIRPY TLGADMHGYN
     TYAGEDGADD RESNPFYGAQ RFCLTLAMSE LLALGMPLHD VVATVTQNAA ALLGLSDEIG
     SLQPGLRADV SVLDLAEGEF RLRDNGGAEA TAAALFVPAL TLKDGRPIEV DSPVVVRPEH
     LH
//
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