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Database: UniProt
Entry: A0A0Q1BLS6_9SPHI
LinkDB: A0A0Q1BLS6_9SPHI
Original site: A0A0Q1BLS6_9SPHI 
ID   A0A0Q1BLS6_9SPHI        Unreviewed;       276 AA.
AC   A0A0Q1BLS6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=orotidine-5'-phosphate decarboxylase {ECO:0000256|ARBA:ARBA00012321};
DE            EC=4.1.1.23 {ECO:0000256|ARBA:ARBA00012321};
GN   ORFNames=AQF98_05540 {ECO:0000313|EMBL:KQC01826.1};
OS   Pedobacter sp. Hv1.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=1740090 {ECO:0000313|EMBL:KQC01826.1, ECO:0000313|Proteomes:UP000050543};
RN   [1] {ECO:0000313|EMBL:KQC01826.1, ECO:0000313|Proteomes:UP000050543}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hv1 {ECO:0000313|EMBL:KQC01826.1,
RC   ECO:0000313|Proteomes:UP000050543};
RA   Ott B.M., Beka L., Graf J., Rio R.;
RT   "Draft Genome Sequence of a Pedobacter sp. Strain Hv1, an Isolate From
RT   Medicinal Leech Mucosal Castings.";
RL   Submitted (OCT-2015) 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};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       UMP from orotate: step 2/2. {ECO:0000256|ARBA:ARBA00004861}.
CC   -!- SIMILARITY: Belongs to the OMP decarboxylase family. Type 2 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008847}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQC01826.1}.
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DR   EMBL; LLWP01000002; KQC01826.1; -; Genomic_DNA.
DR   RefSeq; WP_055130923.1; NZ_LLWP01000002.1.
DR   AlphaFoldDB; A0A0Q1BLS6; -.
DR   STRING; 1740090.AQF98_05540; -.
DR   OrthoDB; 9808470at2; -.
DR   UniPathway; UPA00070; UER00120.
DR   Proteomes; UP000050543; Unassembled WGS sequence.
DR   GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IEA:UniProtKB-EC.
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   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   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050543}.
FT   DOMAIN          16..255
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /evidence="ECO:0000259|SMART:SM00934"
SQ   SEQUENCE   276 AA;  30744 MW;  653FD86E76E6EF43 CRC64;
     MNRKQLFEQI QKKKSFLCIG LDPVLDKLPK HLLKYNDPIL EFNKQLIDAT HDLCVAYKPN
     TAFYESRGVK GWETLVKTWQ HFPKEVFTIA DAKRGDIGNT SAMYAEAFFN EEGSAMSFDS
     ITVAPYMGED SVTPFLAHPD KWVILLALTS NAGSKDFQAK QSEDQKLYEQ VITTSSKWGN
     SDQMMYVVGA TKAEEFENIR RLAPEHFLLV PGVGAQGGSL SAVCKYGLNQ ECGLLVNAAR
     SIIYASDGLD FAEKAREEAL ALQQEMEQIL GAANLL
//
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