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UniProtKB/Swiss-Prot entry A2RJT9


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

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Entry information
Entry name PYRDA_LACLM
Primary accession number A2RJT9
Secondary accession number P54321
Integrated into Swiss-Prot on May 1, 2007
Sequence was last modified on March 6, 2007 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 13)
Name and origin of the protein
Protein name Dihydroorotate dehydrogenase A
Synonyms EC 1.3.3.1
Dihydroorotate oxidase A
DHOdehase A
DHODase A
DHOD A
Gene name
Name: pyrDA
OrderedLocusNames: llmg_0952
From
Lactococcus lactis subsp. cremoris (strain MG1363) [TaxID: 416870] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Lactobacillales; Streptococcaceae; Lactococcus.
Protein existence 3: Inferred from homology;
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 [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).
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
X74206; CAA52279.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AM406671; CAL97544.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_001032274.1; -.
3D structure databases
SMR A2RJT9; 1-311.
ModBase A2RJT9.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0004158; Molecular function: dihydroorotate oxidase activity (inferred from electronic annotation from HAMAP).
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 A2RJT9.
Genome annotation databases
GeneID 4798428; -.
GenomeReviews AM406671_GR; llmg_0952.
KEGG llm:llmg_0952; -.
CMR A2RJT9; llmg_0952.
Other
ProtoNet A2RJT9.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
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 A. PRO_0000285239
ACT_SITE   130   130        Nucleophile (By similarity). 
Sequence information
Length: 311 AA [This is the length of the unprocessed precursor] Molecular weight: 34210 Da [This is the MW of the unprocessed precursor] CRC64: 30157E3C2791CDD7 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLNTTFANAK FANPFMNASG VHCMTIEDLE ELKASQAGAY ITKSSTLEKR EGNPLPRYVD 

        70         80         90        100        110        120 
LELGSINSMG LPNLGFDYYL DYVLKNQKEN AQEGPIFFSI AGMSAAENIA MLKKIQESDF 

       130        140        150        160        170        180 
SGITELNLSC PNVPGKPQLA YDFEATEKLL KEVFTFFTKP LGVKLPPYFD LVHFDIMAEI 

       190        200        210        220        230        240 
LNQFPLTYVN SVNSIGNGLF IDPEAESVVI KPKDGFGGIG GAYIKPTALA NVRAFYTRLK 

       250        260        270        280        290        300 
PEIQIIGTGG IETGQDAFEH LLCGATMLQI GTALHKEGPA IFDRIIKELE EIMNQKGYQS 

       310 
IADFHGKLKS L 

A2RJT9 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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