GenomeNet

Database: UniProt
Entry: A0A1N7SAB0_9BURK
LinkDB: A0A1N7SAB0_9BURK
Original site: A0A1N7SAB0_9BURK 
ID   A0A1N7SAB0_9BURK        Unreviewed;       353 AA.
AC   A0A1N7SAB0;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Dihydroorotase {ECO:0000256|ARBA:ARBA00012860, ECO:0000256|HAMAP-Rule:MF_00219};
DE            Short=DHOase {ECO:0000256|HAMAP-Rule:MF_00219};
DE            EC=3.5.2.3 {ECO:0000256|ARBA:ARBA00012860, ECO:0000256|HAMAP-Rule:MF_00219};
GN   Name=pyrC {ECO:0000256|HAMAP-Rule:MF_00219,
GN   ECO:0000313|EMBL:SIT44292.1};
GN   ORFNames=BN2475_470093 {ECO:0000313|EMBL:SIT44292.1};
OS   Paraburkholderia ribeironis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=1247936 {ECO:0000313|EMBL:SIT44292.1, ECO:0000313|Proteomes:UP000187012};
RN   [1] {ECO:0000313|EMBL:SIT44292.1, ECO:0000313|Proteomes:UP000187012}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=STM7296 {ECO:0000313|EMBL:SIT44292.1,
RC   ECO:0000313|Proteomes:UP000187012};
RA   Song W.-J., Kurnit D.M.;
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate
CC       to dihydroorotate. {ECO:0000256|ARBA:ARBA00002368, ECO:0000256|HAMAP-
CC       Rule:MF_00219}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate;
CC         Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00219,
CC         ECO:0000256|RuleBase:RU003440};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00219,
CC         ECO:0000256|RuleBase:RU003440};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|HAMAP-Rule:MF_00219,
CC       ECO:0000256|RuleBase:RU003440};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       (S)-dihydroorotate from bicarbonate: step 3/3.
CC       {ECO:0000256|ARBA:ARBA00004880, ECO:0000256|HAMAP-Rule:MF_00219,
CC       ECO:0000256|RuleBase:RU003440}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00219}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       DHOase family. Class II DHOase subfamily.
CC       {ECO:0000256|ARBA:ARBA00005631, ECO:0000256|HAMAP-Rule:MF_00219,
CC       ECO:0000256|RuleBase:RU003440}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CYGX02000047; SIT44292.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1N7SAB0; -.
DR   STRING; 1247936.BN2475_470093; -.
DR   OrthoDB; 9808095at2; -.
DR   UniPathway; UPA00070; UER00117.
DR   Proteomes; UP000187012; 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   GO; GO:0019856; P:pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR   CDD; cd01294; DHOase; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   HAMAP; MF_00219; PyrC_classII; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR004721; DHOdimr.
DR   InterPro; IPR002195; Dihydroorotase_CS.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   NCBIfam; TIGR00856; pyrC_dimer; 1.
DR   PANTHER; PTHR43137; DIHYDROOROTASE; 1.
DR   PANTHER; PTHR43137:SF1; DIHYDROOROTASE; 1.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   PIRSF; PIRSF001237; DHOdimr; 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, ECO:0000256|HAMAP-Rule:MF_00219};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00219};
KW   Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975, ECO:0000256|HAMAP-
KW   Rule:MF_00219}; Reference proteome {ECO:0000313|Proteomes:UP000187012};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00219}.
FT   DOMAIN          18..320
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
FT   ACT_SITE        257
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00219"
FT   BINDING         20
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00219"
FT   BINDING         22..24
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00219"
FT   BINDING         22
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00219"
FT   BINDING         48
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00219"
FT   BINDING         106
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00219"
FT   BINDING         106
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00219"
FT   BINDING         143
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00219"
FT   BINDING         143
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00219"
FT   BINDING         181
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00219"
FT   BINDING         229
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00219"
FT   BINDING         257
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00219"
FT   BINDING         261
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00219"
FT   BINDING         273
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00219"
FT   MOD_RES         106
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00219"
SQ   SEQUENCE   353 AA;  38624 MW;  148B691D4D68EB91 CRC64;
     MTASNVSLDS LTLTRPDDWH LHVRDGAMLA AVLPDTARQF GRAIIMPNLK PPVTTTAMAQ
     AYRERIVAAI PAGAKFEPLM TLYLTDNTPP DEIRRARESG FVHGVKLYPA GATTNSDAGV
     TDIMKCAKTL ETMQETGMPL LVHGEVTDSS IDLFDREKVF IDRVMTPLRR AFPALKVVFE
     HITTKDAADY VREAGVAPEL LGATITAHHL LYNRNAIFQG GIRPHYYCLP VLKRETHRVA
     LVEAATSGNP RFFLGTDSAP HPKGLKEHAC GCAGCYTALH ALELYTEAFD QAGALDKLEG
     FASFFGADFY GLPRNVGKVT LRREEWTLPA ELPAGDTPVV PLRGGESIGW RLV
//
DBGET integrated database retrieval system