ID A0A1H7KPZ6_STRJI Unreviewed; 493 AA.
AC A0A1H7KPZ6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Dihydroorotase {ECO:0000313|EMBL:SEK88849.1};
GN ORFNames=SAMN05414137_104151 {ECO:0000313|EMBL:SEK88849.1};
OS Streptacidiphilus jiangxiensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptacidiphilus.
OX NCBI_TaxID=235985 {ECO:0000313|EMBL:SEK88849.1, ECO:0000313|Proteomes:UP000183015};
RN [1] {ECO:0000313|Proteomes:UP000183015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45096 / BCRC 16803 / CGMCC 4.1857 / CIP 109030 / JCM 12277
RC / KCTC 19219 / NBRC 100920 / 33214
RC {ECO:0000313|Proteomes:UP000183015};
RA Varghese N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; FOAZ01000004; SEK88849.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7KPZ6; -.
DR STRING; 235985.SAMN05414137_104151; -.
DR eggNOG; COG0044; Bacteria.
DR OrthoDB; 9803027at2; -.
DR Proteomes; UP000183015; 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 Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR002195; Dihydroorotase_CS.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR NCBIfam; TIGR00857; pyrC_multi; 1.
DR PANTHER; PTHR43668; ALLANTOINASE; 1.
DR PANTHER; PTHR43668:SF2; 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; PS00482; DIHYDROOROTASE_1; 1.
DR PROSITE; PS00483; DIHYDROOROTASE_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000183015}.
FT DOMAIN 84..464
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 493 AA; 52818 MW; A5E98B3F78AE9723 CRC64;
MTELHGQPVH APGNSEQPAH EGPGQEGPGQ EQPYDLVVTG VRLVSGDGVV AGGLAVSSGR
IACLLGPRER PPARRTLDGG GRHLLPGLID SHVHFRTPGL THKEDWAHAG RAAVAGGVTT
VIDMPNTLPP LHTAEEAHRK AELLAGTTLV DHRFHLGVTG DDPSPLRSVG PREATSVKVF
LAGHHTAPDV VRDPAQLEKV FRTAAEAGLR LLLHAEDDAV FGLLDSWRGA PAGYGGYERH
RPRSGGIVAV ARVVELVRRH GTAVHVLHVS SAEEADLLTA AAHTGLPVTF EVTPHHLSFT
ATETSRTGAR ARLSPALRDR SDRERLWQAV VGGEVATLGS DHAPHTRAEK LRPPAEAPPG
LPGVQEMLTA VHTGLRRRAP EDSPDAQLSC LARLLAERPA GLFGLDERKG RLRPGLDADF
VLFDADERWM LAPGAIQSKC GWSAYEGWTM TGRVLRTVRR GETVYSHADG QAEFGSPDGR
WLDARRPGDL VPR
//
