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LOCUS WP_003098837 211 aa linear BCT 04-JUN-2024 ACCESSION WP_003098837 VERSION WP_003098837.1 KEYWORDS RefSeq. SOURCE Pseudomonas ORGANISM Pseudomonas Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae. REFERENCE 1 (residues 1 to 211) AUTHORS Vega,M.C., Zou,P., Fernandez,F.J., Murphy,G.E., Sterner,R., Popov,A. and Wilmanns,M. TITLE Regulation of the hetero-octameric ATP phosphoribosyl transferase complex from Thermotoga maritima by a tRNA synthetase-like subunit JOURNAL Mol Microbiol 55 (3), 675-686 (2005) PUBMED 15660995 REFERENCE 2 (residues 1 to 211) AUTHORS Bovee,M.L., Champagne,K.S., Demeler,B. and Francklyn,C.S. TITLE The quaternary structure of the HisZ-HisG N-1-(5'-phosphoribosyl)-ATP transferase from Lactococcus lactis JOURNAL Biochemistry 41 (39), 11838-11846 (2002) PUBMED 12269828 REFERENCE 3 (residues 1 to 211) AUTHORS Sissler,M., Delorme,C., Bond,J., Ehrlich,S.D., Renault,P. and Francklyn,C. TITLE An aminoacyl-tRNA synthetase paralog with a catalytic role in histidine biosynthesis JOURNAL Proc Natl Acad Sci U S A 96 (16), 8985-8990 (1999) PUBMED 10430882 COMMENT REFSEQ: This record represents a single, non-redundant, protein sequence which may be annotated on many different RefSeq genomes from the same, or different, species. ##Evidence-For-Name-Assignment-START## Evidence Category :: HMM Evidence Accession :: TIGR00070.1 Evidence Source :: JCVI ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..211 /organism="Pseudomonas" /db_xref="taxon:286" gene 1..211 /gene="hisG" Protein 1..211 /product="ATP phosphoribosyltransferase" /EC_number="2.4.2.17" /GO_component="GO:0005737 - cytoplasm [Evidence IEA]" /GO_function="GO:0003879 - ATP phosphoribosyltransferase activity [Evidence IEA]" /GO_process="GO:0000105 - histidine biosynthetic process [Evidence IEA]" /calculated_mol_wt=22714 Region 1..204 /region_name="PBP2_HisGs" /note="The catalytic domain of hetero-octomeric short form HisGs; contains the type 2 periplasmic binding protein fold; cd13595" /db_xref="CDD:270313" Site order(8,36..37,48..49,54,58,60..61,82..87,118,130, 134..139,142,145..146,148,183,191,195,198) /site_type="other" /note="dimer interface [polypeptide binding]" /db_xref="CDD:270313" Site order(139,141,154..156,158..161) /site_type="other" /note="chemical substrate binding site [chemical binding]" /db_xref="CDD:270313" ORIGIN 1 mltialskgr ilddtlplla aagivpsenp dksrkliipt slsdvrlliv ratdvptyve 61 hgaadlgvag kdvlmeyggq glyepldlri ancklmtaga igapepkgrl rvatkfvnva 121 kryyaeqgrq vdviklygsm elaplvglad kiidvvdtgn tlranglepq eliatissrl 181 vvnkasmkmq hgriqslidt lrdavearhr h