Unfortunately due to lack of commercial feasibility, the SkyBLAST service has been suspended from December 1st, 2025.
All subscriptions for paid accounts have been paused. For further information or enquiries, please email [email protected]
LOCUS WP_003142418 456 aa linear BCT 04-JUN-2024 ACCESSION WP_003142418 VERSION WP_003142418.1 KEYWORDS RefSeq. SOURCE Pseudomonas ORGANISM Pseudomonas Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae. REFERENCE 1 (residues 1 to 456) AUTHORS Maynes,J.T., Yuan,R.G. and Snyder,F.F. TITLE Identification, expression, and characterization of Escherichia coli guanine deaminase JOURNAL J Bacteriol 182 (16), 4658-4660 (2000) PUBMED 10913105 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 :: TIGR02967.1 Evidence Source :: JCVI ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..456 /organism="Pseudomonas" /db_xref="taxon:286" gene 1..456 /gene="guaD" Protein 1..456 /product="guanine deaminase" /EC_number="3.5.4.3" /GO_function="GO:0008270 - zinc ion binding [Evidence IEA]" /GO_function="GO:0008892 - guanine deaminase activity [Evidence IEA]" /GO_process="GO:0006147 - guanine catabolic process [Evidence IEA]" /calculated_mol_wt=49578 Region 25..456 /region_name="PRK09228" /note="guanine deaminase; Provisional" /db_xref="CDD:236419" ORIGIN 1 mndavpagnf vpplilhsdh ggsamsssah rgrilhflgd paklgdkawe yfedgllwie 61 hghvraldha tyllpqlpad lpleehpqrl llpgfvdchv hypqlgvias ygtqlldwle 121 thtfpaeqrf adagyaaaqa elfldellrh gtttalvfgt vhavsaeaff qaaqkrrlrm 181 iagkvlmdrn appalcdtaa sgyaesrali erwhgngrlq yavtprfapt sspeqlaaaa 241 rlldeypgvy lhthlsenlk evawvgelfp qaqdyldvyh raglvgersv fahgihlser 301 ecrclahkna alahcpssnl figsglfdlg raqqygirvg igsdvgggts lsllanlada 361 ykiqqlrgts ldpfqalyla tlggaraldl dglvgnflpg readfvaldl aatpmiaqrm 421 ehargladtl fvlntlgddr avaetwvmge rrhvkg