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Database: UniProt
Entry: A1A1G0_BIFAA
LinkDB: A1A1G0_BIFAA
Original site: A1A1G0_BIFAA 
ID   A1A1G0_BIFAA            Unreviewed;       320 AA.
AC   A1A1G0;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   RecName: Full=Orotidine 5'-phosphate decarboxylase {ECO:0000256|HAMAP-Rule:MF_01215};
DE            EC=4.1.1.23 {ECO:0000256|HAMAP-Rule:MF_01215};
DE   AltName: Full=OMP decarboxylase {ECO:0000256|HAMAP-Rule:MF_01215};
DE            Short=OMPDCase {ECO:0000256|HAMAP-Rule:MF_01215};
DE            Short=OMPdecase {ECO:0000256|HAMAP-Rule:MF_01215};
GN   Name=pyrF {ECO:0000256|HAMAP-Rule:MF_01215,
GN   ECO:0000313|EMBL:BAF39543.1};
GN   OrderedLocusNames=BAD_0762 {ECO:0000313|EMBL:BAF39543.1};
OS   Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 /
OS   E194a).
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=367928 {ECO:0000313|EMBL:BAF39543.1, ECO:0000313|Proteomes:UP000008702};
RN   [1] {ECO:0000313|EMBL:BAF39543.1, ECO:0000313|Proteomes:UP000008702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15703 / DSM 20083 / NCTC 11814 / E194a
RC   {ECO:0000313|Proteomes:UP000008702};
RA   Suzuki T., Tsuda Y., Kanou N., Inoue T., Kumazaki K., Nagano S., Hirai S.,
RA   Tanaka K., Watanabe K.;
RT   "Bifidobacterium adolescentis complete genome sequence.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001419, ECO:0000256|HAMAP-
CC         Rule:MF_01215};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       UMP from orotate: step 2/2. {ECO:0000256|ARBA:ARBA00004861,
CC       ECO:0000256|HAMAP-Rule:MF_01215}.
CC   -!- SIMILARITY: Belongs to the OMP decarboxylase family. Type 2 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008847, ECO:0000256|HAMAP-Rule:MF_01215}.
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DR   EMBL; AP009256; BAF39543.1; -; Genomic_DNA.
DR   RefSeq; WP_011743302.1; NC_008618.1.
DR   AlphaFoldDB; A1A1G0; -.
DR   STRING; 367928.BAD_0762; -.
DR   PaxDb; 1680-BADO_0810; -.
DR   KEGG; bad:BAD_0762; -.
DR   HOGENOM; CLU_060704_1_1_11; -.
DR   UniPathway; UPA00070; UER00120.
DR   Proteomes; UP000008702; 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   CDD; cd04725; OMP_decarboxylase_like; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   HAMAP; MF_01215; OMPdecase_type2; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR018089; OMPdecase_AS.
DR   InterPro; IPR011995; OMPdecase_type-2.
DR   InterPro; IPR001754; OMPdeCOase_dom.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   NCBIfam; TIGR02127; pyrF_sub2; 1.
DR   PANTHER; PTHR43375; OROTIDINE 5'-PHOSPHATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43375:SF1; OROTIDINE 5'-PHOSPHATE DECARBOXYLASE; 1.
DR   Pfam; PF00215; OMPdecase; 1.
DR   SMART; SM00934; OMPdecase; 1.
DR   SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
DR   PROSITE; PS00156; OMPDECASE; 1.
PE   3: Inferred from homology;
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP-
KW   Rule:MF_01215};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01215};
KW   Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975, ECO:0000256|HAMAP-
KW   Rule:MF_01215}; Reference proteome {ECO:0000313|Proteomes:UP000008702}.
FT   DOMAIN          52..290
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /evidence="ECO:0000259|SMART:SM00934"
FT   ACT_SITE        112
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01215"
SQ   SEQUENCE   320 AA;  33843 MW;  B68D1A30C6694483 CRC64;
     MDRLIEAIED KQNPSVVGLD PTEALVPNQV VASFAEEIAE QVEDPTEAPA AQLSVAFFEF
     NRAIIDAVAD IVPAVKPQIA MYEALGPAGI DAYSMTCEYA KQQGLYVLGD VKRGDIGSTA
     AAYAHHLSGV NAGEHAFDPW HEDAVTVNPY LGTDGITPFV EAATGADKDI FVLVRTSNPS
     SSELQELELA SGERVYEHVA DLVEGWGAET IGANGYSRVG AVVGATHPEE GKALRARMPH
     TFFLVPGYGA QGGTAQGVAG MFDKDGMGAL VNSSRGIIGA WKKSSKYSES MSADDALDLV
     AESAREAAKD MRDNLRAVLP
//
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