Domains within Bacillus anthracis str. A0248 protein PUR9_BACAA (C3PBN4)

Bifunctional purine biosynthesis protein PurH

Alternative representations: 1 /

Protein length511 aa
Source databaseUniProt
Identifiers PUR9_BACAC, C3L536, PUR9_BACAN, Q81ZG8, Q6I4B5, Q6KY17, PUR9_BACC0, B7JM89, C2TAV1_BACCE, C2TAV1, A0A0K6KV09_BACCE, A0A0K6KV09, A0A0B5XHU2_BACTU, A0A0B5XHU2, A0A0F7RNT9_BACAN, A0A0F7RNT9, C3GDF5_BACTU, C3GDF5, A0A1S9BKX4_KLEPN, A0A1S9BKX4, A0A0A0QA50_BACCE, A0A0A0QA50, K9RYQ8_BACCE, K9RYQ8, A0A0N6Z266_9BACI, A0A0N6Z266, A0A0N6Z253_BACTU, A0A0N6Z253, Q5XWW6_BACCE, Q5XWW6, Q5XWW7_BACAN, Q5XWW7, Q5XWW4_BACTK, Q5XWW4, Q5XWW5_BACTS, Q5XWW5, Q5XWW2_BACMY, Q5XWW2, PUR9_BACAA, C3PBN4

Domain architecture analysis

Display all proteins with similar:

Domain organisationProteins having all the domains as the query in the same order. Additional domains are allowed.
Domain compositionProteins with the same domain composition have at least one copy of each of the domains of the query.

Predicted functional partners

PUR9_BACAA is shown as purH in the network

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The network on the left comes from STRING, a database of known and predicted protein interactions. Displayed here is the evidence view, where different line colors represent the types of evidence for the association.

Open the STRING annotation page for purH

Orthologous groups

Orthology information is taken from eggNOG, a database of orthologous groups of genes. Orthologous groups containing this protein are listed below. This protein is named 261594.GBAA_0298 in eggNOG.

OGTaxonomic classDescription
LCOG0138All organisms (root)phosphoribosylaminoimidazolecarboxamide formyltransferase / IMP cyclohydrolase [EC:2.1.2.3 3.5.4.10],urease accessory protein,phosphoribosylglycinamide/phosphoribosylaminoimidazolecarboxamide formyltransferase [EC:2.1.2.2 2.1.2.3]
5RWAWBacillus cereus group (species group)phosphoribosylaminoimidazolecarboxamide formyltransferase / IMP cyclohydrolase [EC:2.1.2.3 3.5.4.10]
COG0138Bacteria (superkingdom)phosphoribosylaminoimidazolecarboxamide formyltransferase / IMP cyclohydrolase [EC:2.1.2.3 3.5.4.10],carbamoyl-phosphate synthase large subunit [EC:6.3.5.5]
9VRTNFirmicutes (phylum)phosphoribosylaminoimidazolecarboxamide formyltransferase / IMP cyclohydrolase [EC:2.1.2.3 3.5.4.10]
G6306Bacilli (class)phosphoribosylaminoimidazolecarboxamide formyltransferase / IMP cyclohydrolase [EC:2.1.2.3 3.5.4.10]
F32FXBacillales (order)phosphoribosylaminoimidazolecarboxamide formyltransferase / IMP cyclohydrolase [EC:2.1.2.3 3.5.4.10]
F6EFJBacillaceae (family)phosphoribosylaminoimidazolecarboxamide formyltransferase / IMP cyclohydrolase [EC:2.1.2.3 3.5.4.10]
AAW8ABacillus (genus)phosphoribosylaminoimidazolecarboxamide formyltransferase / IMP cyclohydrolase [EC:2.1.2.3 3.5.4.10]

The SMART diagram above represents a summary of the results shown below. Domains with scores less significant than established cutoffs are not shown in the diagram. Features are also not shown when two or more occupy the same piece of sequence; the priority for display is given by SMART > PFAM > PROSPERO repeats > Signal peptide > Transmembrane > Coiled coil > Low complexity. In either case, features not shown in the above diagram are listed in the right side table below, and the reason for their omission is shown in the 'Reason' column.

Confidently predicted domains, repeats, motifs and features:

Outlier homologues and homologues of known structure:

Features NOT shown in the diagram: