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_000082019 406 aa linear BCT 10-JUL-2019 ACCESSION WP_000082019 VERSION WP_000082019.1 KEYWORDS RefSeq. SOURCE Escherichia coli ORGANISM Escherichia coli Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia. REFERENCE 1 (residues 1 to 406) AUTHORS Lal,P.B., Schneider,B.L., Vu,K. and Reitzer,L. TITLE The redundant aminotransferases in lysine and arginine synthesis and the extent of aminotransferase redundancy in Escherichia coli JOURNAL Mol. Microbiol. 94 (4), 843-856 (2014) PUBMED 25243376 REFERENCE 2 (residues 1 to 406) AUTHORS Fraley,C.D., Kim,J.H., McCann,M.P. and Matin,A. TITLE The Escherichia coli starvation gene cstC is involved in amino acid catabolism JOURNAL J. Bacteriol. 180 (16), 4287-4290 (1998) PUBMED 9696780 REFERENCE 3 (residues 1 to 406) AUTHORS Schneider,B.L., Kiupakis,A.K. and Reitzer,L.J. TITLE Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli JOURNAL J. Bacteriol. 180 (16), 4278-4286 (1998) PUBMED 9696779 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 :: BlastRule Evidence Accession :: NBR008163 Evidence Source :: NCBI ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..406 /organism="Escherichia coli" /db_xref="taxon:562" gene 1..406 /gene="astC" Protein 1..406 /product="succinylornithine/acetylornithine transaminase" /EC_number="2.6.1.11" /EC_number="2.6.1.81" /calculated_mol_wt=43549 Region 1..406 /region_name="PRK12381" /note="bifunctional succinylornithine transaminase/acetylornithine transaminase; Provisional" /db_xref="CDD:183486" Site order(104..106,138..139,141,190,223,225..226,252) /site_type="active" /note="inhibitor-cofactor binding pocket [active]" /db_xref="CDD:99735" Site order(105..106,138..139,190,223,226,252) /site_type="other" /note="pyridoxal 5'-phosphate binding site [chemical binding]" /db_xref="CDD:99735" Site 252 /site_type="active" /note="catalytic residue [active]" /db_xref="CDD:99735" ORIGIN 1 msqpitrenf dewmipvyap apfipvrgeg srlwdqqgke yidfaggiav nalghahpel 61 realneqask fwhtgngytn esvlrlakkl idatfadrvf fcnsgaeane aalklarkfa 121 hdrygshksg ivafknafhg rtlftvsagg qpaysqdfap lppdirhaay ndinsasali 181 ddstcavive piqgeggvvp asnaflqglr elcdrhnall ifdevqtgvg rtgelyaymh 241 ygvtpdlltt akalgggfpv gallateeca svmtvgthgt tyggnplasa vagkvlelin 301 tpemlngvkq rhdwfverln iinhryglfn evrglgllig cvlnadyagq akqisqeaak 361 agvmvliagg nvvrfapaln vseeevttgl drfavacehf vsrgss