ID A0A1F6W4L6_9BACT Unreviewed; 407 AA.
AC A0A1F6W4L6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Amidohydrolase {ECO:0000313|EMBL:OGI76860.1};
GN ORFNames=A3B85_01980 {ECO:0000313|EMBL:OGI76860.1};
OS Candidatus Nomurabacteria bacterium RIFCSPHIGHO2_02_FULL_37_13.
OC Bacteria; Candidatus Nomurabacteria.
OX NCBI_TaxID=1801750 {ECO:0000313|EMBL:OGI76860.1, ECO:0000313|Proteomes:UP000178374};
RN [1] {ECO:0000313|EMBL:OGI76860.1, ECO:0000313|Proteomes:UP000178374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate
CC to dihydroorotate. {ECO:0000256|ARBA:ARBA00002368}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC DHOase family. Class I DHOase subfamily.
CC {ECO:0000256|ARBA:ARBA00010286}.
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:OGI76860.1}.
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DR EMBL; MFUA01000017; OGI76860.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6W4L6; -.
DR STRING; 1801750.A3B85_01980; -.
DR Proteomes; UP000178374; Unassembled WGS sequence.
DR GO; GO:0016812; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR002195; Dihydroorotase_CS.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR43668; ALLANTOINASE; 1.
DR PANTHER; PTHR43668:SF4; ALLANTOINASE; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR PROSITE; PS00483; DIHYDROOROTASE_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:OGI76860.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 196..404
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
SQ SEQUENCE 407 AA; 45478 MW; 5C808BF98E1F7109 CRC64;
MLTIEGNIVN IDKVFRGRIE IDQSGIINKI GEPTGDADFI FRDEFIFPGF IDLHVHARED
TSHTQDYKED FITAGQAAIN GGVVAFAEMP NNPVPPIDDA SYEAKNNLTK KSSVTVLLYA
GIGPKTRPLF GKVPYKVFMG PSVGDLFFTS RQSLETALEK YKGQNVTFHC EDPEVLEECK
SGLTHESRRP AKAEILAIDF ALELIERYNL TGKISHCSTI EGIKKIMDAK TRGINVSVEV
TPHHLYFDET MLGDNRKKFQ VNPPIRQSKE NRLALIAALK SGDIDYLATD HAPHTIEEKE
KGISGLTHLD TYGSFIAWLT KEHNFTPQEI ERVCSQNPAN FLNQFIKNKY GEIKEGFVGS
LTIIDMNKPV TITKNILKTK CGWSLFEGMI FPGSVVMTVV KGKTYVK
//
