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Q474U2 (Q474U2_CUPPJ) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Protein attributes

Sequence length448 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate. HAMAP-Rule MF_00220

Cofactor

Binds 2 zinc ions per subunit By similarity. HAMAP-Rule MF_00220

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. HAMAP-Rule MF_00220

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00220

Sequence similarities

Belongs to the DHOase family. Type 2 subfamily. HAMAP-Rule MF_00220

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Metal binding3241Zinc 1 By similarity HAMAP-Rule MF_00220

Sequences

Sequence LengthMass (Da)Tools
Q474U2 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 208196D0FED1E9C0

FASTA44847,783
        10         20         30         40         50         60 
MPTSSQNIPN TPSDTTSQAM KIHIQGGRLI DPAANLDAQQ DLYIAAGKIV GVGSAPADFT 

        70         80         90        100        110        120 
ANKTIDARGL IVCPGLVDLS ARLREPGYEY KATLESEVAA AAAGGVTSLL CPPDTDPVLD 

       130        140        150        160        170        180 
EPGLVEMLKF RARTLNQTHV YPLGALTQGL KGEVLTEMNQ LTEAGCVGFS QAEAPVRNTQ 

       190        200        210        220        230        240 
VLLRALQYAQ TFGFTVWLRP EDPFLGGGVA ASGAVASRLG LSGVSVIAET VRLHTIFELM 

       250        260        270        280        290        300 
RASGARVHLC RLSTAAGLEL VRQAKREGLA VTCDVNIHHV SLTDMDIGYF NSQMRFSPPL 

       310        320        330        340        350        360 
RSARDRDAIV AALADGTIDA LCSDHTPVDD DEKLLPFAEA TPGAIGLELL LPLTLRWAAE 

       370        380        390        400        410        420 
HKVPLKTALA RITSEPARVA GLKAGTLASG AVADICVFDP KEVWKVDRQS IKSQGKNSPW 

       430        440 
LGYEMEGRVR MTLVGGQVVY GNNNHNHH 

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References

[1]"Complete sequence of chromosome 1 of Ralstonia eutropha JMP134."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Goltsman E., Martinez M., Schmutz J., Larimer F., Land M., Lykidis A., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JMP134 / LMG 1197.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000090 Genomic DNA. Translation: AAZ60091.1.
RefSeqYP_294935.1. NC_007347.1.

3D structure databases

ProteinModelPortalQ474U2.
ModBaseSearch...

Protein-protein interaction databases

STRING264198.Reut_A0709.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ60091; AAZ60091; Reut_A0709.
GeneID3609292.
KEGGreu:Reut_A0709.
PATRIC20226879. VBIRalEut24049_1315.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0044.
HOGENOMHOG000219144.
KOK01465.
OMASHHQPHE.
ProtClustDBPRK07627.

Enzyme and pathway databases

BioCycCPIN264198:GIW3-713-MONOMER.
UniPathwayUPA00070; UER00117.

Family and domain databases

HAMAPMF_00220_B. PyrC_type2_B.
InterProIPR004722. DHOase.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
SUPFAMSSF51338. Metalo_hydrolase. 1 hit.
TIGRFAMsTIGR00857. pyrC_multi. 1 hit.
ProtoNetSearch...

Entry information

Entry nameQ474U2_CUPPJ
AccessionPrimary (citable) accession number: Q474U2
Entry history
Integrated into UniProtKB/TrEMBL: September 13, 2005
Last sequence update: September 13, 2005
Last modified: May 1, 2013
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)