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Database: UniProt
Entry: R5QS21_9FIRM
LinkDB: R5QS21_9FIRM
Original site: R5QS21_9FIRM 
ID   R5QS21_9FIRM            Unreviewed;       430 AA.
AC   R5QS21;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   08-MAY-2019, entry version 34.
DE   RecName: Full=Dihydroorotase {ECO:0000256|HAMAP-Rule:MF_00220, ECO:0000256|SAAS:SAAS00853100};
DE            Short=DHOase {ECO:0000256|HAMAP-Rule:MF_00220};
DE            EC=3.5.2.3 {ECO:0000256|HAMAP-Rule:MF_00220, ECO:0000256|SAAS:SAAS00964835};
GN   Name=pyrC {ECO:0000256|HAMAP-Rule:MF_00220};
GN   ORFNames=BN526_01559 {ECO:0000313|EMBL:CCZ29189.1};
OS   Firmicutes bacterium CAG:194.
OC   Bacteria; Firmicutes; environmental samples.
OX   NCBI_TaxID=1263008 {ECO:0000313|EMBL:CCZ29189.1, ECO:0000313|Proteomes:UP000018384};
RN   [1] {ECO:0000313|EMBL:CCZ29189.1, ECO:0000313|Proteomes:UP000018384}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:194 {ECO:0000313|Proteomes:UP000018384};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J.,
RA   Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E.,
RA   Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J.,
RA   Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F.,
RA   Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S.,
RA   Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F.,
RA   Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E.,
RA   Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T.,
RA   MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J.,
RA   Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units
RT   of genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible cyclization of carbamoyl
CC       aspartate to dihydroorotate. {ECO:0000256|HAMAP-Rule:MF_00220,
CC       ECO:0000256|SAAS:SAAS00925093}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-
CC         aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814;
CC         EC=3.5.2.3; Evidence={ECO:0000256|HAMAP-Rule:MF_00220,
CC         ECO:0000256|SAAS:SAAS01124554};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00220};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00220};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
CC       {ECO:0000256|HAMAP-Rule:MF_00220, ECO:0000256|SAAS:SAAS00964833}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases
CC       superfamily. DHOase family. Class I DHOase subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00220, ECO:0000256|SAAS:SAAS00964840}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00220}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:CCZ29189.1}.
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DR   EMBL; CAZT010000086; CCZ29189.1; -; Genomic_DNA.
DR   UniPathway; UPA00070; UER00117.
DR   Proteomes; UP000018384; Unassembled WGS sequence.
DR   GO; GO:0004151; F:dihydroorotase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd01317; DHOase_IIa; 1.
DR   Gene3D; 2.30.40.10; -; 1.
DR   HAMAP; MF_00220_B; PyrC_classI_B; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR004722; DHOase.
DR   InterPro; IPR002195; Dihydroorotase_CS.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR011612; Urease_alpha_N_dom.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   Pfam; PF00449; Urease_alpha; 1.
DR   SUPFAM; SSF51338; SSF51338; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   PROSITE; PS00482; DIHYDROOROTASE_1; 1.
DR   PROSITE; PS00483; DIHYDROOROTASE_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000018384};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00220,
KW   ECO:0000256|SAAS:SAAS00329261};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00220,
KW   ECO:0000256|SAAS:SAAS00329250};
KW   Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00220,
KW   ECO:0000256|SAAS:SAAS01000213};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018384};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00220, ECO:0000256|SAAS:SAAS00964841}.
FT   DOMAIN        2     34       Urease_alpha. {ECO:0000259|Pfam:PF00449}.
FT   DOMAIN       59    427       Amidohydro-rel. {ECO:0000259|Pfam:
FT                                PF01979}.
FT   REGION       67     69       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00220}.
FT   ACT_SITE    314    314       {ECO:0000256|HAMAP-Rule:MF_00220}.
FT   METAL        65     65       Zinc 1; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00220}.
FT   METAL        67     67       Zinc 1; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00220}.
FT   METAL       156    156       Zinc 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00220}.
FT   METAL       156    156       Zinc 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00220}.
FT   METAL       183    183       Zinc 2; via pros nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00220}.
FT   METAL       236    236       Zinc 2; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00220}.
FT   METAL       314    314       Zinc 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00220}.
FT   BINDING      99     99       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00220}.
FT   BINDING     287    287       Substrate; via amide nitrogen and
FT                                carbonyl oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00220}.
FT   BINDING     318    318       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00220}.
SQ   SEQUENCE   430 AA;  46517 MW;  4ACB5FEDF6424A52 CRC64;
     MLLITNGTIV DPVQGIYKGD ILIRDGKIAK IADKIEQTEL KEETESLRII DAAGKKIGPG
     LVDVHVHFRD PGFTHKEDIE TGARAAAAGG FTTVVLMANT KPAVDTKETL SYVLEKGRKT
     GIHVESCACI TKGLAGKELT DMKTLREAGA AGFTDDGIPI LDEALVKAAM EQAKELDVPL
     SFHEEDPAYI ENNGINHGKA SAYYQIGGSD RMAEISLVRR DLELALSTGA AFDVQHISAK
     ESVALVREAK KRAKEMGMDN IHAEATPHHF SLTEEAAIQY GTLAKMNPPL REEADRMAVI
     EGLADGTIDL IATDHAPHSA EEKAKPLTEA PSGIIGLETA FSLAITNLVR PGYLDLPTLF
     ERMSLAPAKL YHLPAGQIKE DMPADLIVFD DAAEVVYEKF ASKSSNSPFT GQKLYGRIEM
     TICEGKEIQK
//
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