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Database: UniProt
Entry: A0A0A1DJV5_NOCSI
LinkDB: A0A0A1DJV5_NOCSI
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ID   A0A0A1DJV5_NOCSI        Unreviewed;       274 AA.
AC   A0A0A1DJV5;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 40.
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:GEB13659.1};
GN   ORFNames=KR76_14645 {ECO:0000313|EMBL:AIY17691.1}, NSI01_19740
GN   {ECO:0000313|EMBL:GEB13659.1};
OS   Nocardioides simplex (Arthrobacter simplex).
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Pimelobacter.
OX   NCBI_TaxID=2045 {ECO:0000313|EMBL:AIY17691.1, ECO:0000313|Proteomes:UP000030300};
RN   [1] {ECO:0000313|EMBL:AIY17691.1, ECO:0000313|Proteomes:UP000030300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM Ac-2033D {ECO:0000313|EMBL:AIY17691.1,
RC   ECO:0000313|Proteomes:UP000030300};
RX   PubMed=25573942;
RA   Shtratnikova V.Y., Schelkunov M.I., Pekov Y.A., Fokina V.V.,
RA   Logacheva M.D., Sokolov S.L., Bragin E.Y., Ashapkin V.V., Donova M.V.;
RT   "Complete Genome Sequence of Steroid-Transforming Nocardioides simplex VKM
RT   Ac-2033D.";
RL   Genome Announc. 3:0-0(2015).
RN   [2] {ECO:0000313|EMBL:GEB13659.1, ECO:0000313|Proteomes:UP000318936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 12069 {ECO:0000313|EMBL:GEB13659.1,
RC   ECO:0000313|Proteomes:UP000318936};
RA   Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT   "Whole genome shotgun sequence of Pimelobacter simplex NBRC 12069.";
RL   Submitted (JUN-2019) 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; CP009896; AIY17691.1; -; Genomic_DNA.
DR   EMBL; BJMC01000009; GEB13659.1; -; Genomic_DNA.
DR   RefSeq; WP_038679288.1; NZ_FOUK01000003.1.
DR   AlphaFoldDB; A0A0A1DJV5; -.
DR   STRING; 2045.KR76_14645; -.
DR   KEGG; psim:KR76_14645; -.
DR   eggNOG; COG0284; Bacteria.
DR   HOGENOM; CLU_060704_0_0_11; -.
DR   OrthoDB; 9808470at2; -.
DR   UniPathway; UPA00070; UER00120.
DR   Proteomes; UP000030300; Chromosome.
DR   Proteomes; UP000318936; Unassembled WGS sequence.
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; 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.
PE   3: Inferred from homology;
KW   Decarboxylase {ECO:0000256|HAMAP-Rule:MF_01215};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01215};
KW   Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01215};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030300}.
FT   DOMAIN          16..261
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /evidence="ECO:0000259|SMART:SM00934"
FT   ACT_SITE        95
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01215"
SQ   SEQUENCE   274 AA;  28391 MW;  C8AA291C55FDD687 CRC64;
     MTFGARLVAA VADRGPFCVG IDPHASLLHA WGYDDDVAGL ERFALGAVEA VAPHCSVIKP
     QSAFYERFGS RGVAVLERVI EAGRAAGALV LLDIKRGDIG STSQAYADAY LDPASPLACD
     AVTVSPYLGF GSLQPFVDTA EKFDAGLFVL AATSNKEGPE VQEAVTGGRT VSATVLDHLR
     RLNADAVPLG SFGAVVGATL EDDRGLDLAF NGPILAPGYG EQGGTTADLR RIFGAGVRNV
     LATSSRGVLR LGPDPAALAG AVRRSNDELR ELLG
//
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