PYRF_LACAC
ID PYRF_LACAC Reviewed; 235 AA.
AC Q5FJB3;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=LBA1386;
OS Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=272621;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700396 / NCK56 / N2 / NCFM;
RX PubMed=15671160; DOI=10.1073/pnas.0409188102;
RA Altermann E., Russell W.M., Azcarate-Peril M.A., Barrangou R., Buck B.L.,
RA McAuliffe O., Souther N., Dobson A., Duong T., Callanan M., Lick S.,
RA Hamrick A., Cano R., Klaenhammer T.R.;
RT "Complete genome sequence of the probiotic lactic acid bacterium
RT Lactobacillus acidophilus NCFM.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3906-3912(2005).
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; CP000033; AAV43211.1; -; Genomic_DNA.
DR RefSeq; WP_003548039.1; NC_006814.3.
DR RefSeq; YP_194242.1; NC_006814.3.
DR PDB; 3TFX; X-ray; 2.19 A; A/B=1-235.
DR PDBsum; 3TFX; -.
DR AlphaFoldDB; Q5FJB3; -.
DR SMR; Q5FJB3; -.
DR STRING; 272621.LBA1386; -.
DR EnsemblBacteria; AAV43211; AAV43211; LBA1386.
DR GeneID; 56942965; -.
DR KEGG; lac:LBA1386; -.
DR PATRIC; fig|272621.13.peg.1311; -.
DR eggNOG; COG0284; Bacteria.
DR HOGENOM; CLU_067069_1_1_9; -.
DR OMA; NFKIFLD; -.
DR BioCyc; LACI272621:G1G49-1360-MON; -.
DR UniPathway; UPA00070; UER00120.
DR Proteomes; UP000006381; 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..235
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /id="PRO_0000241868"
FT ACT_SITE 62
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 10
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 33
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 60..69
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 123
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 215
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:3TFX"
FT HELIX 14..22
FT /evidence="ECO:0007829|PDB:3TFX"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:3TFX"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:3TFX"
FT HELIX 36..42
FT /evidence="ECO:0007829|PDB:3TFX"
FT HELIX 44..52
FT /evidence="ECO:0007829|PDB:3TFX"
FT STRAND 56..63
FT /evidence="ECO:0007829|PDB:3TFX"
FT HELIX 67..78
FT /evidence="ECO:0007829|PDB:3TFX"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:3TFX"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:3TFX"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:3TFX"
FT HELIX 93..106
FT /evidence="ECO:0007829|PDB:3TFX"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:3TFX"
FT HELIX 127..132
FT /evidence="ECO:0007829|PDB:3TFX"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:3TFX"
FT HELIX 140..153
FT /evidence="ECO:0007829|PDB:3TFX"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:3TFX"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:3TFX"
FT HELIX 166..173
FT /evidence="ECO:0007829|PDB:3TFX"
FT STRAND 175..181
FT /evidence="ECO:0007829|PDB:3TFX"
FT HELIX 200..205
FT /evidence="ECO:0007829|PDB:3TFX"
FT STRAND 209..213
FT /evidence="ECO:0007829|PDB:3TFX"
FT HELIX 215..218
FT /evidence="ECO:0007829|PDB:3TFX"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:3TFX"
FT HELIX 223..234
FT /evidence="ECO:0007829|PDB:3TFX"
SQ SEQUENCE 235 AA; 25404 MW; 892076F9C45D7B1F CRC64;
MDRPVIVALD LDNEEQLNKI LSKLGDPHDV FVKVGMELFY NAGIDVIKKL TQQGYKIFLD
LKMHDIPNTV YNGAKALAKL GITFTTVHAL GGSQMIKSAK DGLIAGTPAG HSVPKLLAVT
ELTSISDDVL RNEQNCRLPM AEQVLSLAKM AKHSGADGVI CSPLEVKKLH ENIGDDFLYV
TPGIRPAGNA KDDQSRVATP KMAKEWGSSA IVVGRPITLA SDPKAAYEAI KKEFN