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UniProtKB/Swiss-Prot entry P54322

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PYRDB_LACLM
Primary accession number P54322
Secondary accession number A2RK90
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on May 1, 2007 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 64)
Name and origin of the protein
Protein name Dihydroorotate dehydrogenase B, catalytic subunit
Synonyms EC 1.3.3.1
Dihydroorotate oxidase B
DHOdehase B
DHODase B
DHOD B
Gene name
Name: pyrDB
OrderedLocusNames: llmg_1106
From
Lactococcus lactis subsp. cremoris (strain MG1363) [TaxID: 416870] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Lactobacillales; Streptococcaceae; Lactococcus.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8021180 [NCBI, ExPASy, EBI, Israel, Japan]
Andersen P.S., Jansen P.J.G., Hammer K.;
"Two different dihydroorotate dehydrogenases in Lactococcus lactis.";
J. Bacteriol. 176:3975-3982(1994).
[2]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8759867 [NCBI, ExPASy, EBI, Israel, Japan]
Andersen P.S., Martinussen J., Hammer K.;
"Sequence analysis and identification of the pyrKDbF operon from Lactococcus lactis including a novel gene, pyrK, involved in pyrimidine biosynthesis.";
J. Bacteriol. 178:5005-5012(1996).
[3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1128/JB.01768-06; PubMed=17307855 [NCBI, ExPASy, EBI, Israel, Japan]
Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C., Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P., van Sinderen D., Kok J.;
"The complete genome sequence of the lactic acid bacterial paradigm Lactococcus lactis subsp. cremoris MG1363.";
J. Bacteriol. 189:3256-3270(2007).
[4]
 CHARACTERIZATION.
DOI=10.1074/jbc.271.46.29359; PubMed=8910599 [NCBI, ExPASy, EBI, Israel, Japan]
Nielsen F.S., Andersen P.S., Jensen K.F.;
"The B form of dihydroorotate dehydrogenase from Lactococcus lactis consists of two different subunits, encoded by the pyrDb and pyrK genes, and contains FMN, FAD, and [FeS] redox centers.";
J. Biol. Chem. 271:29359-29365(1996).
[5]
 X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
DOI=10.1016/S0969-2126(00)00530-X; PubMed=11188687 [NCBI, ExPASy, EBI, Israel, Japan]
Rowland P., Noerager S., Jensen K.F., Larsen S.;
"Structure of dihydroorotate dehydrogenase B: electron transfer between two flavin groups bridged by an iron-sulphur cluster.";
Structure 8:1227-1238(2000).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X74207; CAA52280.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AM406671; CAL97700.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_001032420.1; -.
3D structure databases
PDB
1EP1; X-ray; 2.20 A; A=1-311.[ExPASy / RCSB / EBI]
1EP2; X-ray; 2.40 A; A=1-311.[ExPASy / RCSB / EBI]
1EP3; X-ray; 2.10 A; A=1-311.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1EP1; -.
1EP2; -.
1EP3; -.
ModBase P54322.
Protein-protein interaction databases
IntAct P54322; -.
Ontologies
GO
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.
Family and domain databases
HAMAP MF_00224; -; 1.
PBIL [Tree]
InterPro IPR013785; Aldolase_TIM.
IPR012135; DHO_DHase_1_2.
IPR005720; DHO_DHase_1_core.
IPR001295; Dihydroorotate_DHase_core.
Graphical view of domain structure.
Gene3D G3DSA:3.20.20.70; Aldolase_TIM; 1.
Pfam PF01180; DHO_dh; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000164; DHO_oxidase; 1.
TIGRFAMs TIGR01037; pyrD_sub1_fam; 1.
PROSITE PS00911; DHODEHASE_1; 1.
PS00912; DHODEHASE_2; 1.
BLOCKS P54322.
Genome annotation databases
GeneID 4798332; -.
GenomeReviews AM406671_GR; llmg_1106.
KEGG llm:llmg_1106; -.
CMR P54322; llmg_1106.
Other
ProtoNet P54322.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Cytoplasm; Flavoprotein; FMN; Oxidoreductase; Pyrimidine biosynthesis.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   311  311     Dihydroorotate dehydrogenase B, catalytic subunit. PRO_0000148396
ACT_SITE   135   135        Nucleophile. 
CONFLICT   123   123        A -> R (in Ref. 1; CAA52280 and 2). 
CONFLICT   239   239        V -> D (in Ref. 1; CAA52280 and 2). 
CONFLICT   255   255        D -> V (in Ref. 1; CAA52280 and 2). 
CONFLICT   266   266        A -> R (in Ref. 1; CAA52280 and 2). 
HELIX   5     7  3      
STRAND   9    11  3      
STRAND   14    22  9      
HELIX   31    34  4      
HELIX   39    41  3      
STRAND   45    50  6      
STRAND   63    66  4      
STRAND   69    72  4      
HELIX   81    86  6      
HELIX   88    95  8      
STRAND   101   105  5      
HELIX   110   120  11      
STRAND   126   132  7      
STRAND   135   137  3      
TURN   138   142  5      
HELIX   145   147  3      
HELIX   149   162  14      
STRAND   167   170  4      
HELIX   179   187  9      
STRAND   191   195  5      
STRAND   199   201  3      
TURN   206   209  4      
STRAND   210   213  4      
STRAND   218   222  5      
HELIX   223   225  3      
HELIX   226   237  12      
STRAND   244   246  3      
HELIX   253   262  10      
STRAND   265   269  5      
HELIX   272   275  4      
HELIX   279   293  15      
HELIX   299   308  10      
Sequence information
Length: 311 AA [This is the length of the unprocessed precursor] Molecular weight: 32930 Da [This is the MW of the unprocessed precursor] CRC64: 1854517E5B585BB9 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MTENNRLSVK LPGLDLKNPI IPASGCFGFG EEYAKYYDLN KLGSIMVKAT TLHPRFGNPT 

        70         80         90        100        110        120 
PRVAETASGM LNAIGLQNPG LEVIMTEKLP WLNENFPELP IIANVAGSEE ADYVAVCAKI 

       130        140        150        160        170        180 
GDAANVKAIE LNISCPNVKH GGQAFGTDPE VAAALVKACK AVSKVPLYVK LSPNVTDIVP 

       190        200        210        220        230        240 
IAKAVEAAGA DGLTMINTLM GVRFDLKTRQ PILANITGGL SGPAIKPVAL KLIHQVAQVV 

       250        260        270        280        290        300 
DIPIIGMGGV ANAQDVLEMY MAGASAVAVG TANFADPFVC PKIIDKLPEL MDQYRIESLE 

       310 
SLIQEVKEGK K
P54322 in FASTA format

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