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UniProtKB/Swiss-Prot entry Q2GL89

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

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Entry information
Entry name PYRC_ANAPZ
Primary accession number Q2GL89
Secondary accession numbers None
Integrated into Swiss-Prot on March 18, 2008
Sequence was last modified on March 21, 2006 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 22)
Name and origin of the protein
Protein name Dihydroorotase
Synonyms DHOase
EC 3.5.2.3
Gene name
Name: pyrC
OrderedLocusNames: APH_0245
From
Anaplasma phagocytophilum (strain HZ) [TaxID: 212042] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; Anaplasmataceae; Anaplasma; phagocytophilum group.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1371/journal.pgen.0020021; PubMed=16482227 [NCBI, ExPASy, EBI, Israel, Japan]
Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V., Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M., Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., Nelson W.C., Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P., Daugherty S.C., Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H., Selengut J.D., Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R., Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H.;
"Comparative genomics of emerging human ehrlichiosis agents.";
PLoS Genet. 2:208-222(2006).
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
CP000235; ABD43938.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_504862.1; -.
3D structure databases
ModBase Q2GL89.
Enzyme and pathway databases
BioCyc APHA212042:APH_0245-MON; -.
Ontologies
GO
GO:0004151; Molecular function: dihydroorotase activity (inferred from electronic annotation from HAMAP).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from HAMAP).
GO:0006221; Biological process: pyrimidine nucleotide biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00220; -; 1.
PBIL [Tree]
InterPro IPR006680; Amidohydro_1.
IPR004722; DHOmult.
IPR002195; Dihydroorotase_CS.
Graphical view of domain structure.
Pfam PF01979; Amidohydro_1; 1.
Pfam graphical view of domain structure.
ProDom PD000518; DHOase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR00857; pyrC_multi; 1.
PROSITE PS00482; DIHYDROOROTASE_1; 1.
PS00483; DIHYDROOROTASE_2; 1.
BLOCKS Q2GL89.
Genome annotation databases
GeneID 3931083; -.
GenomeReviews CP000235_GR; APH_0245.
KEGG aph:APH_0245; -.
NMPDR fig|212042.5.peg.233; -.
TIGR APH_0245; -.
Phylogenomic databases
HOGENOM Q2GL89; -.
Other
ProtoNet Q2GL89.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Hydrolase; Metal-binding; Pyrimidine biosynthesis; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   447  447     Dihydroorotase. PRO_0000325581
METAL   84    84        Zinc 1 (By similarity). 
METAL   86    86        Zinc 1 (By similarity). 
METAL   164   164        Zinc 1; via carbamate group (By similarity). 
METAL   164   164        Zinc 2; via carbamate group (By similarity). 
METAL   201   201        Zinc 2 (By similarity). 
METAL   255   255        Zinc 2 (By similarity). 
METAL   328   328        Zinc 1 (By similarity). 
MOD_RES   164   164        N6-carboxylysine (By similarity). 
Sequence information
Length: 447 AA [This is the length of the unprocessed precursor] Molecular weight: 48529 Da [This is the MW of the unprocessed precursor] CRC64: B09D15AE95C66DC9 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MVSERQTWSL LQGGQCNEYT VAYINARIID PASGTDYKGY LLTRGKEILD FGPGFFDPNG 

        70         80         90        100        110        120 
AAFAASEVVD CNGHVLMPGI VDLHVHLREP GGEHKETVDT GSRAAAAGGV TTVVCQPNTI 

       130        140        150        160        170        180 
PRLENVLVAK YLKMRALESS CVNIEFYGAV TKSDGELCDM ASLKDAGALG FTDDGLPVMN 

       190        200        210        220        230        240 
ALYMKRAFEY AQDLDVVVAQ HAEDCNLSDG GCINEGLVSR ELGLKGIPDI SESIMVSRDI 

       250        260        270        280        290        300 
QLLREVPGAH YHVLHISTKK ALDIVRAAKR EGLRVTCEVT PHHFLLNESA VLEHGTMAKM 

       310        320        330        340        350        360 
NPPLRTEEDR LSMISGLEDG TIDCIATDHA PHAAQEKTRP ISCCAFGIVG LETLLPLSLE 

       370        380        390        400        410        420 
LYHNAGMSLM DVLSKLTSKP AEIVRLPRGK IAKGLVADLV IFDLEHVWTI DTAKFSSKSK 

       430        440 
NSPFQGRKVK GKVLRTVVSG KTVYRAE
Q2GL89 in FASTA format

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