PYRC_METTH
ID PYRC_METTH Reviewed; 431 AA.
AC O27199; Q50488;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2003, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Dihydroorotase {ECO:0000255|HAMAP-Rule:MF_00220};
DE Short=DHOase {ECO:0000255|HAMAP-Rule:MF_00220};
DE EC=3.5.2.3 {ECO:0000255|HAMAP-Rule:MF_00220};
GN Name=pyrC {ECO:0000255|HAMAP-Rule:MF_00220}; OrderedLocusNames=MTH_1127;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=7929010; DOI=10.1128/jb.176.20.6384-6391.1994;
RA Pihl T.D., Sharma S., Reeve J.N.;
RT "Growth phase-dependent transcription of the genes that encode the two
RT methyl coenzyme M reductase isoenzymes and N5-
RT methyltetrahydromethanopterin:coenzyme M methyltransferase in
RT Methanobacterium thermoautotrophicum delta H.";
RL J. Bacteriol. 176:6384-6391(1994).
CC -!- FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate
CC to dihydroorotate. {ECO:0000255|HAMAP-Rule:MF_00220}.
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:0000255|HAMAP-Rule:MF_00220};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00220};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00220};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 3/3. {ECO:0000255|HAMAP-
CC Rule:MF_00220}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC DHOase family. Class I DHOase subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_00220}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB85616.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE000666; AAB85616.1; ALT_INIT; Genomic_DNA.
DR EMBL; U09990; AAA73440.1; -; Genomic_DNA.
DR PIR; A69017; A69017.
DR PIR; T45151; T45151.
DR RefSeq; WP_048060972.1; NC_000916.1.
DR AlphaFoldDB; O27199; -.
DR SMR; O27199; -.
DR STRING; 187420.MTH_1127; -.
DR MEROPS; M38.972; -.
DR PRIDE; O27199; -.
DR EnsemblBacteria; AAB85616; AAB85616; MTH_1127.
DR GeneID; 1471535; -.
DR KEGG; mth:MTH_1127; -.
DR PATRIC; fig|187420.15.peg.1104; -.
DR HOGENOM; CLU_015572_1_1_2; -.
DR OMA; QHAQEPR; -.
DR UniPathway; UPA00070; UER00117.
DR Proteomes; UP000005223; Chromosome.
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 Gene3D; 2.30.40.10; -; 1.
DR HAMAP; MF_00220_A; PyrC_classI_A; 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 Pfam; PF01979; Amidohydro_1; 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 Hydrolase; Metal-binding; Pyrimidine biosynthesis; Reference proteome;
KW Zinc.
FT CHAIN 1..431
FT /note="Dihydroorotase"
FT /id="PRO_0000147273"
FT ACT_SITE 290
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 55
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 57..59
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 57
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 89
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 290
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 294
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 308..309
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT MOD_RES 139
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT CONFLICT 1..2
FT /note="MF -> SL (in Ref. 2; AAA73440)"
FT /evidence="ECO:0000305"
FT CONFLICT 44
FT /note="G -> A (in Ref. 2; AAA73440)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="F -> N (in Ref. 2; AAA73440)"
FT /evidence="ECO:0000305"
FT CONFLICT 195..201
FT /note="ARPPLAE -> CKTSPRR (in Ref. 2; AAA73440)"
FT /evidence="ECO:0000305"
FT CONFLICT 242..243
FT /note="CE -> SQ (in Ref. 2; AAA73440)"
FT /evidence="ECO:0000305"
FT CONFLICT 343
FT /note="A -> P (in Ref. 2; AAA73440)"
FT /evidence="ECO:0000305"
FT CONFLICT 395..404
FT /note="GPVMTIVRGR -> ARHDHCQGQ (in Ref. 2; AAA73440)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 431 AA; 47946 MW; FFE05E8B923ADAF9 CRC64;
MFDLSLENCR VDRDLTVNIG VDDGKIVQIS RGRIDASEKI DLKGYFVLPG LIDAHVHFRD
PGLEYKEDFR TGSMAAAHGG FSTVLDMPNT VPPADNAAEF ERKIRIGERK SVVDFGLHAG
FRSVSDVKGI LRFMPASFKV FMDLTGISTV DGLFRELKDL SAPVPVTVHC ENRDVVMKSM
KELKDRSDPS AYALARPPLA EEVSVAEVLA LSIHHEHPVH ICHLSTVKAL QLVEPFREYV
TCEVTPHHLL LDSGAFRRFG TMVKTNPPLR PPESRIYPEF LDRINIIGTD HAPHGIEEKR
KGIWDAPPGI PNLEVVLKLL LTLVSKGRMS LSTIRRMLAE EPARIFGLRS KGRIAEGMDA
DFTVIDLKET GRIRSDEFYS KAHYTPFEGF SYTGGPVMTI VRGRAVMRDG EVLEGNGRYI
PAEHDGKHGS A
