PYRF_CAMJE
ID PYRF_CAMJE Reviewed; 279 AA.
AC Q9PIC1; Q0PBC9;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Orotidine 5'-phosphate decarboxylase {ECO:0000255|HAMAP-Rule:MF_01200};
DE EC=4.1.1.23 {ECO:0000255|HAMAP-Rule:MF_01200};
DE AltName: Full=OMP decarboxylase {ECO:0000255|HAMAP-Rule:MF_01200};
DE Short=OMPDCase {ECO:0000255|HAMAP-Rule:MF_01200};
DE Short=OMPdecase {ECO:0000255|HAMAP-Rule:MF_01200};
GN Name=pyrF {ECO:0000255|HAMAP-Rule:MF_01200}; OrderedLocusNames=Cj0381c;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
CC -!- FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate
CC (OMP) to uridine 5'-monophosphate (UMP). {ECO:0000255|HAMAP-
CC Rule:MF_01200}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + orotidine 5'-phosphate = CO2 + UMP;
CC Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01200};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC UMP from orotate: step 2/2. {ECO:0000255|HAMAP-Rule:MF_01200}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01200}.
CC -!- SIMILARITY: Belongs to the OMP decarboxylase family. Type 1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01200}.
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DR EMBL; AL111168; CAL34531.1; -; Genomic_DNA.
DR PIR; C81381; C81381.
DR RefSeq; WP_002858700.1; NC_002163.1.
DR RefSeq; YP_002343818.1; NC_002163.1.
DR PDB; 3RU6; X-ray; 1.80 A; A/B/C/D=1-279.
DR PDBsum; 3RU6; -.
DR AlphaFoldDB; Q9PIC1; -.
DR SMR; Q9PIC1; -.
DR IntAct; Q9PIC1; 23.
DR STRING; 192222.Cj0381c; -.
DR PaxDb; Q9PIC1; -.
DR PRIDE; Q9PIC1; -.
DR EnsemblBacteria; CAL34531; CAL34531; Cj0381c.
DR GeneID; 904704; -.
DR KEGG; cje:Cj0381c; -.
DR PATRIC; fig|192222.6.peg.372; -.
DR eggNOG; COG0284; Bacteria.
DR HOGENOM; CLU_067069_1_1_7; -.
DR OMA; NFKIFLD; -.
DR UniPathway; UPA00070; UER00120.
DR Proteomes; UP000000799; Chromosome.
DR GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_01200_B; OMPdecase_type1_B; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR014732; OMPdecase.
DR InterPro; IPR018089; OMPdecase_AS.
DR InterPro; IPR001754; OMPdeCOase_dom.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR PANTHER; PTHR32119:SF2; PTHR32119:SF2; 1.
DR Pfam; PF00215; OMPdecase; 1.
DR SMART; SM00934; OMPdecase; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR TIGRFAMs; TIGR01740; pyrF; 1.
DR PROSITE; PS00156; OMPDECASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Decarboxylase; Lyase; Pyrimidine biosynthesis;
KW Reference proteome.
FT CHAIN 1..279
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /id="PRO_0000134535"
FT ACT_SITE 60
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 8
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 30
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 58..67
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 117
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 206
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 207
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:3RU6"
FT HELIX 12..21
FT /evidence="ECO:0007829|PDB:3RU6"
FT TURN 22..24
FT /evidence="ECO:0007829|PDB:3RU6"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:3RU6"
FT HELIX 33..39
FT /evidence="ECO:0007829|PDB:3RU6"
FT HELIX 41..50
FT /evidence="ECO:0007829|PDB:3RU6"
FT STRAND 54..61
FT /evidence="ECO:0007829|PDB:3RU6"
FT HELIX 65..76
FT /evidence="ECO:0007829|PDB:3RU6"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:3RU6"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:3RU6"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:3RU6"
FT HELIX 91..101
FT /evidence="ECO:0007829|PDB:3RU6"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:3RU6"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:3RU6"
FT HELIX 121..128
FT /evidence="ECO:0007829|PDB:3RU6"
FT HELIX 132..145
FT /evidence="ECO:0007829|PDB:3RU6"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:3RU6"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:3RU6"
FT HELIX 158..164
FT /evidence="ECO:0007829|PDB:3RU6"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:3RU6"
FT HELIX 192..197
FT /evidence="ECO:0007829|PDB:3RU6"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:3RU6"
FT HELIX 207..210
FT /evidence="ECO:0007829|PDB:3RU6"
FT HELIX 215..226
FT /evidence="ECO:0007829|PDB:3RU6"
SQ SEQUENCE 279 AA; 32331 MW; C395A4569A7338A8 CRC64;
MKLCVALDLS TKEECLQLAK ELKNLDIWLK VGLRAYLRDG FKFIEELKKV DDFKIFLDLK
FHDIPNTMAD ACEEVSKLGV DMINIHASAG KIAIQEVMTR LSKFSKRPLV LAVSALTSFD
EENFFSIYRQ KIEEAVINFS KISYENGLDG MVCSVFESKK IKEHTSSNFL TLTPGIRPFG
ETNDDQKRVA NLAMARENLS DYIVVGRPIY KNENPRAVCE KILNKIHRKN ISENDIEQNY
EVIQQKEWDM CNHFEEWIKT RPDKEHALKE FYAKCGIKY
