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LOCUS WP_002898202 396 aa linear BCT 01-JAN-2025 ACCESSION WP_002898202 VERSION WP_002898202.1 KEYWORDS RefSeq. SOURCE Klebsiella ORGANISM Klebsiella Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group. REFERENCE 1 (residues 1 to 396) AUTHORS Christen,P. and Mehta,P.K. TITLE From cofactor to enzymes. The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes JOURNAL Chem Rec 1 (6), 436-447 (2001) PUBMED 11933250 REFERENCE 2 (residues 1 to 396) AUTHORS Schneider,G., Kack,H. and Lindqvist,Y. TITLE The manifold of vitamin B6 dependent enzymes JOURNAL Structure 8 (1), R1-R6 (2000) PUBMED 10673430 REFERENCE 3 (residues 1 to 396) AUTHORS Mehta,P.K. and Christen,P. TITLE The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes JOURNAL Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000) PUBMED 10800595 REFERENCE 4 (residues 1 to 396) AUTHORS Alexander,F.W., Sandmeier,E., Mehta,P.K. and Christen,P. TITLE Evolutionary relationships among pyridoxal-5'-phosphate-dependent enzymes. Regio-specific alpha, beta and gamma families JOURNAL Eur J Biochem 219 (3), 953-960 (1994) PUBMED 8112347 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 :: Conserved Domain (CDD) Evidence Accession :: Domain architecture ID 10013160 Evidence Source :: NCBI SPARCLE ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..396 /organism="Klebsiella" /db_xref="taxon:570" Protein 1..396 /product="amino acid aminotransferase" /EC_number="2.6.1.-" /GO_function="GO:0008483 - transaminase activity [Evidence IEA]" /GO_function="GO:0030170 - pyridoxal phosphate binding [Evidence IEA]" /calculated_mol_wt=43408 Region 1..396 /region_name="PRK09257" /note="aromatic amino acid transaminase" /db_xref="CDD:181731" Site order(102..104,130,183,214,243,245..246,254) /site_type="other" /note="pyridoxal 5'-phosphate binding site [chemical binding]" /db_xref="CDD:99734" Site order(105,140,207,252..254,290,293) /site_type="other" /note="homodimer interface [polypeptide binding]" /db_xref="CDD:99734" Site 246 /site_type="active" /note="catalytic residue [active]" /db_xref="CDD:99734" ORIGIN 1 mfenitaapa dpilgladlf raddrpekin lgigvykdet gktpvltsvk kaeqyllene 61 ttknylgidg ipefgrctqe llfgkgnaii adkrartaqt pggtgalrva adflakntdv 121 krvwvsnpsw pnhksvftsa glevreyayy daanhaldfd gllaslneaq agdvvlfhgc 181 chnptgidpt ldqwqqlaql svekgwlplf dfayqgfarg leedaeglra faalhkellv 241 assysknfgl ynervgactl vaadqetvdr afsqmksvir anysnppahg asvvatilsn 301 dalraiweqe ltdmrqriqr mrllfvntlq ekgasrdfsf isqqngmfsf sgltkeqvlr 361 lreefaiyav asgrinvagm tpdnmaplce aivavl